Academic Year 2017: 21 August 2017 – 27 November 2017 ... · 3 Course Syllabus and Lesson Plan SCBM 282 Medical Biochemistry Laboratory: From Molecules to Cells (Chemical processes

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Course Syllabus and Lesson PlanSCBM 281

Medical Biochemistry: From Molecules to Cells (Chemical processes in living system)

Academic Year 2017: 21 August 2017 – 27 November 2017

Course Title: Medical Biochemistry, From Molecules to Cells

Course Code: SCBM 281

Total Credit: 3(3-0-6)

Pre-Requisite:Duration: First semester

Course Homepage:http://www.sc.mahidol.ac.th/scbc/webboard/index.php

Course Description:Structures and functions of biomolecules, protein folding, protein functions, bio-catalysis,

enzyme kinetics, citric acid cycle, electron transport and oxidative phosphorylation, anabolism

and catabolism of biomolecules in normal and some important pathological stages, regulation

of metabolic pathways, flow of genetic information, gene regulation, and molecular techniques

with medical applications.

Course Objectives:At the end of this course, the students will be able to

1. explain chemical processes occurred in living system, structure and functional relationship of

biomolecules 2. point out the regulation of metabolic pathways governing the life of a cell

3. know and understand energy metabolism, biosynthesis and degradation in both normal and

some important pathological stages

4. emphasize fundamental of genome organization, flow of genetic information and gene

regulation

5. learn the principle of molecular techniques relevant to medical applications.

Course Outlines:See schedule on page

Teaching MethodsLecture

Teaching Media• Text book Lehninger, Principle of Biochemistry, 4

th or 5

th edition,

• CAI, VDO, PowerPoint and/or transparency presentation, can be self-study via web site:

http://www.sc.mahidol.ac.th/scbc/webboard/index.php

Evaluation of Student AchievementGrading system from midterm and final examination

• Midterm written examination (MCQ) 30%

• Final written examination (MCQ) 70%

Total 100%

Students who get a total grade more than 50% are considered successful for this course.

Course EvaluationQuestionnaire about contents, teaching processes, examinations and instructor performance.

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Required Textbook• Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 4

th or 5

th edition,

Worth, New York

Other References1. Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990.

2. John, W. Baynes and Marek H. Dominiczak, Medical Biochemistry, 2nd edition, Elsevier

Mosby, 2005

3. Other equivalent biochemistry textbooks.

InstructorsLecturer from Department of Biochemistry, Pharmacology, Physiology and Clinician and guest

lecturers from outside Faculty of Science

Course CoordinatorsAsist. Prof. Dr. Jamorn Somana

Department of Biochemistry, Faculty of Science, Mahidol University

Tel: 0-2201-5601 and 0-2201-5468

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Course Syllabus and Lesson PlanSCBM 282

Medical Biochemistry Laboratory: From Molecules to Cells (Chemical processes in living system)

Academic Year 2017: 29 August 2017 – 14 November 2017

Course Title: Medical Biochemistry Laboratory

Course Code: SCBM 282

Total Credit: 1(0-3-1)

Pre-Requisite: Duration: First semester

Course Homepage: http://www.sc.mahidol.ac.th/scbc/webboard/index.php

Course Description: Determination of LDH enzyme activity by spectrophotometric method, Determination of liver

enzyme activities, DNA isolation and PCR amplification followed with analysis of DNA by gel

electrophoresis technique, structures and functions of biomolecules, protein folding, protein

functions, bio-catalysis, enzyme kinetics, TCA cycle, electron transport and oxidative

phosphorylation, anabolism and catabolism of biomolecules in normal and pathological stages,

regulation of metabolic pathways, flow of genetic information, gene regulation, and molecular

techniques with medical applications. Starvation

Course Objectives: At the end of this course, the students will be able to

1. have a laboratories skill on basic techniques in structure and functional relationship of

biomolecules

2. gain the knowledge and understand the way to analysis the experimental data

3. work together or have group activities relevant to chemical processes occurred in living

system and medical applications

4. acquire necessary knowledge through current available resources and analyze critical

problems and data obtained.

Course Outlines:See schedule on page

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Teaching Methods: Laboratory, Group study, Discussion and assignment

1. Laboratories: Compulsory

There are 4 laboratory exercises designed to broaden the students’ skill and knowledge. These

are 1) determination of LDH enzyme activity and studying LDH enzyme kinetics by

spectrophotometric method 2) determination of liver enzyme activities 3) Determination of

cholesterol and triglyceride in serum lipoproteins 4) DNA isolation, PCR amplification and

analysis of DNA by gel electrophoresis technique.

2. Small Group or Conferences: Compulsory

There are 3 small group discussions. The sessions involve discussion on problem sets related to

the topics SCID 141 and some clinical cases. Student presentation and discussion will be

focused and all sessions will have either pre- or post discussion quizzes.

3. Problem-Based Learning: Compulsory

Problem-based scenario will be given to initiate group activities in the discussion and self-study

sessions to find out a possible explanation for the problem. Developments of conceptual

thinking skill and integration of information are the main objective.

4. Tutorials: Not Compulsory

There are 3 tutorial periods to cover the basic concepts of the course. Tutorial period is

provided to help students better understand the topics and/or clarify some points after their

self- or group-study. Therefore, students are expected to go through the topics and prepare

questions prior to each tutorial discussion. Questions for each tutorial session can be posted at

the web-board (see course homepage) or can be submitted directly to the lecturer(s). All

tutorials will be held at lecture hall.

5. CAI (CD and VDO): Compulsory

There are 1 CAI media available in this course, i.e. structure folding and build block, high

throughput automated system, and molecular diagnosis, PCR and sequencing technique. These

learning materials will be installed in the computer system and the students can access and

study during free time. One CAI-media on PCR and DNA sequencing techniques is used in a

class discussion.

Teaching Media: • Laboratory manual of the course

• Text book Lehninger, Principle of Biochemistry, 4th or 5

th edition,

• CAI, VDO, PowerPoint and transparency presentations, can be self study via web site:

http://www.sc.mahidol.ac.th/scbc/webboard/index.php

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Evaluation of student achievement: Grading system from written examination and work assignments or performance in the

activities

Process 80% Small group (5% x3) 15%

PBL (10% x 2) 20%

Laboratories (10% x 4) 40%

CAI (5%) 5%

Knowledge 20% From written examination (Midterm 10% and Final 10%)

Out of the total 100%, students who get a grade more than 60% are considered successful

for this course

Course Evaluation: Questionnaire about contents, teaching processes, examinations and Instructor performance.

Required Textbook• Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 4

th or 5

th edition,

Worth, New York

Other References: 1. Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990.

2. John, W. Baynes and Marek H. Dominiczak, Medical Biochemistry, 2nd

edition, Elsevier

Mosby, 2005

3. Other equivalent biochemistry textbooks.

Instructors: Lecturer from Department of Biochemistry

Course Coordinators: Assist. Prof. Dr. Jamorn Somana

Department of Biochemistry, Faculty of Science, Mahidol University

Tel: 0-2201-5601 and 0-2201-5468

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SCBM 281, 282 Schedule for the First Semester, Year 2017, Student Group SCBM

Day Date Time Activity Room Instructor

Monday 21 Aug 17

8.30-10.30Course Orientation

Lecture 1: DNA Replication and Repair SC1-161 Jamorn(BC), Laran(BC)

10.30-12.30 Lecture 2: RNA and Protein Synthesis SC1-161 Laran (BC)

Tuesday 22 Aug 17

13.30-15.30 Lecture 3: Gene Expression and Regulation SC1-161 Laran (BC)

15.30-17.30 Lecture 4: DNA Technology SC1-161 Laran (BC)

Monday 28 Aug 17

8.30-10.30 Lecture 5: Structure and Functions of Biomolecules SC1-161 Kittisak (BC)

10.30-12.30 Lecture 6: Protein Structure and Concept of Folding SC1-161 Kittisak (BC)

Tuesday 29 Aug 17 13.30-15.30 CAI: Molecular Diagnostic, PCR and DNA Sequencing SC1-161 Laran (BC) & TA

Monday 4 Sep 17

8.30-10.30 Lecture 7 Biocatalysis and Enzyme Kinetics SC1-161 Kittisak (BC)

10.30-12.30Lecture 8: Protein Structure and Function /

Molecular AssemblySC1-161 Kittisak (BC)

Tuesday 5 Sep 17

13.30-14.30Lab 1: DNA Isolation, PCR, Electrophoresis – Brief

Lab SC3 Lab

Laran (BC) and TA

14.30-16.30Lab 1: DNA Isolation, PCR, Electrophoresis –

Experiment SC3 Lab

Monday 11 Sep 17 9.30-11.30 Lecture 9: Carbohydrate Metabolism SC1-161 Wilai(BC)

MU congregation day 12 September 2017

Monday 18 Sep 17 9.30-11.30Conference 1: Active Learning Lesson: Molecular

Technology in MedicineSC1-161 Laran (BC) & TA

Tuesday 19 Sep 17

13.30-14.30 Lab 2: Enzyme LDH – Brief Lab

SC3 Lab Kittisak (BC) & TA

14.30-16.30 Lab 2: Enzyme LDH – Experiment

Monday 25 Sep 17 9.30-11.30Lecture 10: Citric Acid Cycle / Oxidative

Phosphorylation SC1-161 Tuangporn(BC)

Tuesday 26 Sep 17 13.30-15.30 Conference 2: Hemoglobin Structure and Function SC1-161 Kittisak (BC) & TA

Monday 2 Oct 17

8.30-10.30 Lecture 11: Amino Acids Metabolism SC1-161 Wilai(BC)

10.30-12.30 Lecture 12: Nutrition SC1-161 Wilai(BC)

Tuesday 3 Oct 17 13.30-15.30 PBL 1: Hunger StrikeSC1-

161+Jamorn(BC), Tuangporn(BC) and TA

Monday 9 Oct 17 9.30-11.30 Lecture 13: Nucleotide metabolism SC1-161 Tuangporn(BC)

Tuesday 10 Oct 17 13.30-15.30Tutorial 1: Q&A Structure & Function, Gene

regulation & DNA technology SC1-161 Kittisak(BC), Laran(BC),

Midterm Examination 16-20 October 2017

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Day Date Time Activity Room Instructor

Chulalongkorn Memorial Day 23 October 2017

Tuesday 24 Oct 17 13.30-15.30 Conference 3: Active Learning Lesson: Diabetes SC1-161 Jamorn(BC) and TA

Monday 30 Oct 17

8.30-10.30 Lecture 14: Lipid Metabolism SC1-161 Jamorn(BC)

10.30-12.30 Lecture 15: Heme and Minerals Metabolism SC1-161 Jamorn(BC)

Tuesday 31 Oct 17

13.30-14.30 Lab 3: Determination of Serum Lipids – Brief Lab SC3 Lab

Jamorn(BC) and TA

14.30-16.30 Lab 3: Determination of Serum Lipids – Experiment SC3 Lab

Monday 6 Nov 17 9.30-11.30Lecture 16: Integration and Regulation of

MetabolismSC1-161 Jamorn(BC)

Tuesday 7 Nov 17 13.30-15.30 PBL 2: Hunger StrikeSC1-

161+Jamorn(BC), Tuangporn(BC) and TA

Monday 13 Nov 17 9.30-11.30 Lecture 17: Biochemistry Knowledge and Medicine SC1-161 Jamorn(BC)

Tuesday 14 Nov 17

13.30-14.30Lab 4: Determination of Liver Enzyme Activities –

Brief LabSC3 Lab

Tuangporn(BC) and TA

14.30-16.30Lab 4: Determination of Liver Enzyme Activities –

ExperimentSC3 Lab

Monday 27 Nov 17 9.30-11.30 Tutorial 2: Q&A Metabolism, Medical Application SC1-161Wilai(BC), Tuangporn(BC),

Jamorn(BC)

Final Examination 12-22 December 2017

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LESSON PLAN

Lecture 1: DNA replication and repair

Instructor: Laran T. Jensen, Biochemistry, Faculty of Science

Date/Time: Monday, 21 August 2017, 8.30-10.30

Room: SC1-161

Learning Objectives: Students should be able to

1. list factors required for DNA replication

2. explain the functions of enzymes and protein in DNA replication

3. define the meanings of leading and lagging strand DNA synthesis, and okazaki fragment

4. explain the concepts of mutation and repair mechanism

Content Outlines: 1. Flow of genetic material, the central dogma

2. DNA replication, semi-conservative replication, origin of replication

3. replication fork Leading and lagging strand synthesis, okazaki fragment

4. Functions of proteins and enzymes required for DNA replication

5. Mutation and repair mechanism

Leading questions:

- What is the semi-conservative DNA replication?

- How can replication of mammalian DNA which is much bigger than the prokaryotic

DNA being carried out in just a few minutes?

- What are the functions of topoisomerase, helicase, single stranded binding protein,

primase, DNA polymerase and DNA ligase?

- What are the functions of DNA polymerase I and III?

- Why DNA replication is so accurate?

Learning Organization: 1. Lecture 110 min.

2. Q&A 10 min.

3. Study from the course textbook

Learning Materials provided: • List of suggested readings.

Student Assessment: Multiple-choice questions with short (written) explanations.

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LESSON PLAN

Lecture 2: RNA and protein synthesis


Date/Time: Monday, 21 August 2017, 10.30-12.30

Room: SC1-161

Learning objectives: Students should be able to

RNA metabolism

1. list components required for transcription

2. explain the component and function of RNA polymerase

3. explain the function of promoter

4. describe steps of transcription

5. describe posttranscriptional modification of RNAs

Protein synthesis

1. explain the terms “codon”, anticodon”, wobble base and meaning of genetic code

2. discuss the factors require for translation

3. explain steps of translation

4. explain how the peptide bonds are form between amino acids during translation

5. explain the actions of some antibiotics on protein synthesis

6. discuss how nuclear encoded proteins are transported to organelles

Content Outlines: RNA metabolism

1. Transcription (initiation, elongation and termination)

2. functions of various proteins and enzymes required for transcription

3. Promoter recognition and RNA polymerase

4. RNA processing:mRNA, rRNA and tRNA

5. Reverse transcriptase

Leading questions:

- What determine the boundary of gene?

- What is the function of TATA-box?

- What are the functions of sigma factor and core RNA polymerase?

- What is the importance of 5’-capping, intron removal and 3’-polyadenylation?

- Why can some single-copied genes produce multiple isoforms of encoded proteins?

Protein synthesis

1 Genetic code, triplet codon, open reading frame

2. Ribosome structure and component

3. tRNA

4. Translation initiation, elongation and termination

5. Effect of antibiotics on protein synthesis

6. Protein targeting

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Leading questions:

- What is the meaning of non-overlapping triplet codon?

- How is mRNA stabilized on the ribosome?

- What is a maximum number of genetic codes that are recognized by tRNA?

- How does tRNAs carry amino acids?

- What is the function of peptidyl transferase?

- Why does protein synthesis consume high energy?

- How are many proteins imported to plasma membrane, mitochondria and nucleus?

- Why do some antibiotics affect protein synthesis of prokaryote but not eukaryote


2. Q&A 10 min.


Learning Materials provided: • List of suggested readings.


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LESSON PLAN

Lecture 3: Gene Expression and Regulation


Date/Time: Tuesday, 22 August 2017, 13.30-15.30

Room: SC1-161

Learning Objective:Students are expected to accomplishing the following tasks:

1. Describe the molecular basis of transcription and translation control.

2. Apply knowledge to explain normal developmental physiology and pathogenesis.

Content Outline:1. Classification and basis of transcription control.

1.1 Gene organization and control.

1.2 Transcription control in virus and bacteria.

2. Eukaryotic transcription control.

2.1 Components and complexity of transcription control in eukaryotes.

2.2 RNA processing.

2.3 DNA and histone modifications.

2.4 The role of non-coding RNAs in gene regulation.

3. Classification and basis of translation control.

3.1 Control of translation machinery assembly.

3.2 Diseases caused by translation defects.

Learning Organization:1. Lecture presentation.

2. Questions and answers.

Reading Material:1. Class handout.

2. Lehninger Principles of Biochemistry 5th edition, 2009.

Leading questions: Principles of gene regulation

• What are the different levels of gene regulation in living cells and what are their roles ? (P.

1081)

• What is the advantage of regulating gene expression at the transcriptional level ? (P. 1082)

• What are ‘constitutive’ and ‘regulated’ gene expression ? How different are their roles ? (P.

1082)

• What are ‘induction’ and ‘repression’ of gene expression ? (P. 1082)

• What are the roles of transcription factors ? How many different types are there ? How do

they work to regulate transcription ? (P. 1082-1083)

• What are ‘positive’ and ‘negative’ regulations ? How are they different ? How do they

regulate gene expression ? (P. 1084)

Prokaryotic gene expression

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• What is an ‘operon’ ? What are the components of an operon, their function, and

organization within the operon ? (P. 1085)

• How is ‘Lac Operon’ subjected to ‘negative regulation’ by lactose ? What happens in the

absence/presence of lactose ? (P. 1085-1087)

• What are the ‘inducer’ of Lac Operon ? What are the roles of lactose, allolactose and IPTG in

regulating Lac Operon ? (P. 1087)

• How is ‘Lac Operon’ subjected to ‘positive regulation’ by glucose ? What is ‘catabolite

repression’ ? (P. 1093-1094)

• What happens when both lactose and glucose are present ? (P. 1093-1094)

Eukaryotic gene expression

• What makes gene regulation in prokaryote and eukaryote different ? (P. 1102) 57

• What are ‘heterochromatin’ and ‘euchromatin’ ? How do they regulate gene expression in

eukaryote ? Do they have a role in regulating gene expression in prokaryote ? (P. 1102)

• How does chromatin remodeling occur ? What is the role in regulating eukaryotic gene

expression ? (P. 1103)

• What is the meaning of ‘positive regulation’ ? (P. 1103)

• Why are most eukaryotic genes under ‘positive’ regulation ? (P. 1104)

• How are eukaryotic genes regulated by intercellular signals such as steroid hormones ? (P.

1108)

Student Assessment: MCQ or written exam.

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LESSON PLAN

Lecture 4: DNA Technology



Room: SC1-161

Learning Objectives:Students are able to

1. define the techniques of gene cloning and the methods of creating restriction maps

2. recite polymerase chain reactions, DNA or genome sequencing, gene expressions and

proteomes

3. look at the practical benefits and human issues of genetic engineering

Content Outlines:1. DNA cloning: The basics (Chapter 9)

Leading Questions:

- What is DNA cloning or definition of DNA cloning? (pp.306-307)

- What is the function of restriction enzyme? What is the structure of palindromic

sequence? (pp.308-309)

- How many types of cloning vectors? (pp. 311-315)

- How difference between gDNA library and cDNA library? (pp.318-319)

2. Polymerase chain reactions (Chapter 9)

Leading Questions:

- What is the key step of PCR? (pp.319-321)

- What is a definition of primer? (pp.319-321)

3. DNA or genome sequencing (Chapter 8 and 9)

Leading Questions:

- How many methods to determine DNA sequences? (pp. 296-299)

- Which strategy use to study DNA or genome sequences? (pp. 321-322)

4. Gene expression and proteomes (Chapter 9)

Leading Questions:

- How can we know the protein function? (pp.325)

- Which methods do we use to study proteomes? (pp.326)

- What are DNA microarrays and protein chips? (pp. 326-328)

5. Genome alterations and new products of Biotechnology and Medicine (Chapter 9)

Leading Question:

- Give an example on DNA technology yields new products and challenges? (pp.336-338)


2. Q&A 10 min.


Reference:Lehninger Principles of Biochemistry by Nelson and Cox, 4

th Edition, 2005


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LESSON PLAN

Lecture 5: Structure and Function of Biomolecules

Instructor: Kittisak Yokthongwattana, Biochemistry Faculty of Science

Date/Time: Monday 28 August 2017, 8.30-10.30

Room: SC1-161

Learning Objectives: At the end of this lecture, students will be able to

1. Carbohydrates and Glycobiology

1.1 identify the structure and characteristics of common carbohydrates

1.2 differentiate various classes of carbohydrate and their functions

1.3 discuss on the major carbohydrate components of extracellular matrices

1.4 differentiate storage and structural carbohydrates in animal and plant

2. Nucleotides and Nucleic Acids

2.1. understand basic structures of nucleotides, DNA, RNA and derivatives

2.2. differentiate various types/structures of nucleic acids

2.3. discuss basic chemistry of nucleic acids

2.4. discuss various functions of nucleotides

3. Lipids

3.1 understand basic structure and chemical properties of lipids

3.2 discuss on the chemistry and structures of membrane-forming lipids

3.3 discuss roles of lipids

4. Biological Membranes and Transports

4.1. discuss on biological membrane composition and architecture

4.2. understand dynamics of lipid-bilayer membranes

4.3. discuss on transport of substances across biological membranes

Reference: • Ferrier, R.,D., Lippincott’s Illustrated Reviews Biochemistry, 6

th edtion, Lippincott Williams &

Wilkins (ASP)

• Lehninger Principles of Biochemistry by Nelson and Cox, 4th Edition 2005

Content Outlines: 1. Carbohydrates and Glycobiology

1.1 Monosaccharides and disaccharides Chapter 7, page 238-246

1.2 Polysaccharides Chapter 7, page 247-255

1.3 Glycoconjugates: proteoglycans, Chapter 7, page 255-261

glycoproteins and glycolipids

1.4 Carbohydrates as informational molecules Chapter 7, page 261-267

Leading Questions:

• What is the difference between aldose and ketose sugars? (P. 239)

• What is the difference between D and L sugar? (P. 240)

• What are the different isoforms/derivatives of glucose and their biological significance? (P.

241-244)

• What are reducing sugars and how do you test for it? (P. 244-245)

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• What are the major storage polysaccharides in nature? What are they composed of? (P.

247-248)

• Which carbohydrates are components of extracellular matrix that serves as lubricants in

joints of vertebrates? (253-254)

• What are lectins and how do they involved with carbohydrate molecules? (P. 262-267)

2. Nucleotides and Nucleic Acids

2.1 Basic properties of nucleotides & nucleic acids Chapter 8, page 273-279

2.2 Nucleic Acid Structure Chapter 8, page 279-291

2.3 Nucleic acid chemistry Chapter 8, page 291-300

2.4 Other functions of nucleotides Chapter 8, page 300-302

Leading Questions:

• What are the different types of nucleotides and their common names? (P. 273-275)

• What are major groove and minor groove in the DNA structure? (P. 282)

• What are the differences between DNA and RNA?

• Why is DNA more stable than RNA?

• How does UV light cause DNA damage? (P. 694-695)

• Besides being a building block of nucleic acids, what are other functions of nucleotides? (P.

300-302)

3. Lipids

3.1 Storage lipids Chapter 10, page 343-348

3.2 Structural lipid in membranes Chapter 10, page 348-357

3.3 Lipids as signals, cofactors, and pigments Chapter 10, page 357-363

Leading Questions:

• What are fatty acids and how do they differ from one another? (P. 343-344)

• What are triglycerides and waxes? What are their roles in nature? (P. 345-348)

• What are the different types of membrane-forming lipids? (P. 348-350)

• What is the role of membrane lipids in blood group determination? (P. 354)

• What are sterols? Give some examples of their derivatives. (P. 354-355, 359)

• What are eicosanoids and what are their roles? (P. 358-359)

4. Biological Membranes and Transports

4.1 Composition and architecture of membranes Chapter 11, page 369-380

4.2 Membrane dynamics Chapter 11, page 380-389

4.3 Solute transport across membranes Chapter 11, page 389-416

Leading Questions:

• How biological membranes are formed from lipid molecules? (P. 370-373)

• How do different proteins associate with lipid-bilayer membranes? (P. 373-376)

• What are examples of plasma membrane proteins involved in membrane surface adhesion?

(P. 385-386)

• What are the different types of solute transport across biological membranes? (P. 389-393)

• What is the role of GLUT4 protein in the removal of blood sugar? (P. 396)

• How are Na+ and K

+ transported across the lipid membranes? (P. 398-399)

Learning Organization: • Lecture is given

• Students review and study the learning materials according to the outlined content

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Learning Materials provided: • Lippincott’s Illustrated Reviews Biochemistry, 6

th edtion

• Lehninger Principles of Biochemistry by Nelson and Cox, 4th Edition 2005

• Slide presentation provided on the web site

Student Assessment: • Self-assessments are provided on the web or at the end of each chapter.

• MCQ with short explanation exam

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LESSON PLAN

Lecture 6: Protein Structure and Concept of Folding


Date/Time: Monday 28 August 2017, 10.30-12.30

Room: SC2-203

Learning Objectives: Students are able to

• describe unique properties of water that are crucial for properties, structural assembly, and

functions of macromolecules and thus for a living system.

• differentiate various types of chemical interactions in aqueous solution.

• describe general features of amino acids as building blocks of proteins.

• recognize chemical properties of amino acids whose chemical structures are given.

• describe the general concept of formation of protein 3D structure and chemical interactions

involved.

• describe importance of weak-force interactions in protein folding.

• recognize importance of water in protein folding.

Content Outlines: • Chemical interactions in aqueous solution.

• Proteins as major components of cells.

• Proteins are polymers of amino acids.

• Natural amino acids with diverse chemical properties.

• Hierarchy of protein 3D structure.

• Importance of weak-force interactions in protein folding.

Learning Organization: • The session consists of a three-hour lecture using PowerPoint presentation that aims to give

students overview and basic concept about protein structure and amino acids, as well as

weak-forced interaction involved in protein structure stabilization and folding.

• Students are encouraged to read a textbook for more information about protein structure

and amino acids.

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Learning Materials provided: • Hand-out of PowerPoint presentation.

References: • Amino Acid Quiz (http://info.bio.cmu.edu/Courses/BiochemMols/PQuiz/PQInst.html)

• Chapter on protein and amino acids in any new biochemistry textbook such as (but not

limited to):

• Ferrier, R.,D., Lippincott’s Illustrated Reviews Biochemistry, 6th edtion, Lippincott Williams &

Wilkins (ASP)

• Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 2nd edition,

Worth, New York, 1993.

• Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990.

• Branden, C., and Tooze, J., Introduction to Protein Structure, Garland, New York, 1991.

Student Assessment: • Multiple-choice questions with short (written) explanations.

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LESSON PLAN

CAI: Molecular Diagnostic, PCR and DNA Sequencing



Room: SC1-161

Learning Objectives:Students will be able to

1. describe PCR, DNA sequencing and southern blotting processes and explain the molecular

basis of these processes

2. describe DNA fingerprint and its applications

CAI Outlines:1. PCR

2. DNA sequencing

3. Southern blotting

4. DNA fingerprinting

Learning Organization:1. Study the learning materials (animation and VDO) in advance

2. Discussion with the group and hand in questions or points to discuss 24 hour before class.

3. In class, discussion and answering questions 50 min

Learning Materials:1. CAI programs installed in computers in MDL 2 and 3

2. Suggested websites

References:• CD The Cell (Cooper), Molecular Cell Biology (Lodish) or Lehninger

• Website: www.dnalc.org/resources/BiologyAnimationLibrary.htm

Student Assessment:• Students will be asked by tutoring team members to perform some tasks or answer

questions related to the CAI practice session.

• Pre- or Post-test during all processes of learning

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LESSON PLAN

Lecture 7: Biocatalysis and Enzyme Kinetics


Date/Time: Monday 4 September 2017, 8.30-10.30

Room: SC1-161

Learning Objectives:

Student will be able to

1. Introduction to Enzymes

1.1. explain basic and common properties of enzymes.

1.2. describe thermodynamics of reactions catalyzed by enzymes and compare to the

reactions without catalysis.

1.3. describe factors specifying enzyme active site and specificity.

1.4. describe types of reactions catalyzed by enzymes

1.5. explain concepts and roles of cofactors in catalysis

2. Introduction to Enzyme Kinetics

2.1. describe a plot of initial rates versus substrate concentrations

2.2. derive the initial rate equation according to the Michaelis-Menten model.

2.3. use graphical methods to calculate Km, Vmax, kcat, kcat/Km and explain the meanings

of these parameters.

2.4. explain different types of enzyme inhibition.

3. Example of Enzyme Catalysis

1.1 describe hydrolysis of a peptide bond without catalysis by proteases.

1.2 write reaction mechanism of Chymotrypsin-catalyzed reactions

1.3 describe factors facilitating catalysis in Chymotrypsin

4. Regulatory Enzymes

4.1. explain feedback inhibition.

4.2. describe the role of covalent modification in controlling catalysis.

4.3. explain functional roles of allosteric enzymes.

4.4. describe functions of zymogen or proenzymes.

Content Outline 1. Introduction to Enzymes

1.1 What is enzyme?

1.2 Thermodynamics of reactions catalyzed by enzymes

1.3 Enzyme active site and specificity

1.4 Types of reactions catalyzed by enzymes

1.2 Cofactor

2. Introduction to Enzyme Kinetics

2.1 A plot of initial rates versus substrate concentrations

2.2 Derivation of Michaelis-Menten model

2.3 Km, Vmax, kcat, kcat/Km

2.4 Enzyme inhibition

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3. Example of Enzyme Catalysis

3.1 Hydrolysis of a peptide bond

3.2 Mechanism of Chymotrypsin-catalyzed reactions

3.3 Factors facilitating catalysis in Chymotrypsin

4. Regulatory Enzymes

4.1 Feedback inhibition

4.2 Covalent modification

4.3 Allosteric enzymes

4.4 Zymogen or proenzymes


2. Q&A 10 min.


References: • Ferrier, R.,D., Lippincott’s Illustrated Reviews Biochemistry, 6

th edtion, Lippincott Williams &

Wilkins (ASP)

• Lehninger Principle of Biochemistry 4th edition, 2005 Chapter 6 Enzymes

• Biochemistry by Berg, Tymoczko, and Stryer, 6th Edition, 2006 Chapter 8-9


22

LESSON PLAN

Lecture 8: Protein Structure and Function/ Molecular Assembly



Room: SC1-161

Learning Objectives: Students will be able to

• differentiate various types of chemical interactions in aqueous solution.

• describe importance of weak-force interactions in assembly of biomolecules.

• recognize importance of water in molecular assembly.

• distinguish specific recognition from non-specific binding.

Content Outlines: • Various types of molecular assembly.

Non-specific binding.

Specific recognition.

• Cellular compartmentalization and fluid mosaic membrane structure.

• Chemical interactions involved in assembly of biomolecules by examples.

Ion channel.

Chaperone.

Learning Organization: • The session consists of a two-hour lecture using PowerPoint presentation that aims to give

students overview and basic concept about biomolecular assembly.

• Students are encouraged to read the provided material and any textbook for more

information about molecular assembly and various complexes of biomolecules.

Learning Materials provided: • Hand-out of PowerPoint presentation.

References: • Chapters on biomolecular complexes and membrane-associated proteins in any new

biochemistry textbook such as (but not limited to):

• Ferrier, R.,D., Lippincott’s Illustrated Reviews Biochemistry, 6th edtion, Lippincott Williams &

Wilkins (ASP)Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 2nd

edition, Worth, New York, 1993.

• Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990.


23

LESSON PLAN

Laboratory 1: DNA Isolation, PCR and Gel electrophoresis


Date/Time: Tuesday, 5 September 2017, 13.30-15.30

Room: SC3-lab

Learning Objectives: Students should be able to

1. isolate genomic DNA from human leukocytes

2. describe principle of amplify target DNA by Polymerase chain reaction (PCR)

3. describe the relationship among MW of biomolecules, type of supporters and electrical field

4. visualize migrated DNA in an agarose gel electrophoresis

5. determine MW or size in basepair or shape of DNA molecules

Content Outlines: 1. Principle and how to isolate genomic DNA from human leukocytes

2. Principle and how to do the PCR reaction.

3. Principle and how to use electrophoresis technique

4. Determination of DNA molecules both in qualitative and quantitative analysis

Learning Organization: 1. Studying the laboratory manual provided in advance.

2. Lab preview 30 min, Room L04.

3. Pre-test or homework to prepare a flow chart.

4. Hand on laboratory experiment.

5. Laboratory discussion

Learning Materials Provided: 1. Laboratory manual

2. Chemicals, equipments for laboratory test.

References: 1. Laboratory manual

2. Lehninger, L. A., Nelson, D. L., and Cox, M. M., Principles of Biochemistry, 2nd edition,


3. Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990.

Student Assessment: For processes evaluation: 5% per lab

• Quiz or pre-test and Attendance 30%

• Report (by Group) 40%

• Post test (Lab discussion) 30%

24

LESSON PLAN

Lecture 9: Carbohydrate Metabolism

Instructor: Wilai Noonpakdee, Biochemistry, Faculty of Science


Room: SC1-161


Students should be able to

1. describe metabolic map, catabolic vs anabolic pathway and discuss its regulation(short vs

long term)

2. describe glycolysis(the hub of carbohydrate metabolism) pathway, aerobic vs anaerobic

glycolysis, glycolysis reactions from glucose to pyruvate; regulations, energy yield, other

monosacharides and disaccharides metabolism including fructose/lactose.

3. overview gluconeogenesis; its substrates, unique reactions; reciprocal regulation of

glycolysis and gluconeogenesis (allosteric/hormones/substrate availability) ie under well

fed/starvation condition.

4. describe glycogen metabolism: glycogengenesis;glycogenolysis reactions. Regulations

to meet body need together with a common pathological signs in glycogen storage

diseases.

5. identify functional points in the body to oxidize glucose in pentose phosphate pathway

(hexose monophosphate shunt) and cause of damage when this pathway is limited.

Content Outlines:

1. Metabolic map; catabolic and anabolic pathways and their products; metabolism

regulation(short vs long term)(intra/intercellular/hormones)

2. Transport of glucose into cells, glycolysis pathways from glucose to pyruvate(10 reactions:

two phases), key regulatory steps and enzymes (allosteric,hormones insulin/glucagon)

hexokinase I, IV PFK1, pyruvate kinase ; energy yields, metabolism of other mono and

disaccharides fructose and lactose and some diseases involve.

3. Fates of pyruvate in aerobic and anerobic conditions; reduction of pyruvate to lactate.

4. Gluconeogenesis:role, substrates, unique reactions( 3 from 10 of glycolysis reactions),

regulation during fasting via key regulatory enzymes.

5. Roles of pentose phosphate pathway in generating ribose 5 phosphate and usage of

NADPH; G6PD role in RBC and its deficiency

6. Glycogen metabolism; liver and muscle glycogen, synthesis of glycogen(UDP-gluclose,

glycogen synthase, primer, elongation), glycogen degradation(glycogen phosphorylase,

debranching enzyme ) , regulation well fed/fasting state; Glycogen storage diseases( type

Ia, <Von Gierke>, type II, III, V

Leading Questions: Metabolism:

1. Rate of pathway in metabolism may be influenced by what mechanisms (page 94)

Glycolysis

1. How does glucose enter cell? GLUT 1-4 , tissue specific explain..(p 97)

2. What is the principle of cells to make sugar to be entered in metabolic pathway in the form

of phosphate sugar?

25

3. Explain how glucokinase (Hexokinase IV) is responsible for maintaining blood glucose after

eating a meal? Via Km , Vmax.. not Hexokinase (I-III) (p 98-99).

4. What is 2,6 bisphosphate and its role during fasting and well-fed stead? Under glucagon and

insulin; which enzyme is regulated in both glycolysis/gluconeogenesis

5. Why does pyruvate kinase deficiency is profound in RBC but not liver or other cells? (pate

103-3).

6. What tissues that have lactate as major fate of pyruvate ? Explain the ratio of NADH/NAD+

and lactate formation (p 103)

7. Pyruvate kinase can be de or phosphorylated via insulin and glucagon. In the well fed state

pyruvate kinase should be activated/inactivated and in what form? (P 102).

8. Explain why lactic acidosis occur in myocardial infarction condition or in a shock person?

(page 104) What is oxygen debt?

9. Why do many adult Asian people get diarrhea after drinking fresh milk?

10. What enzymes are defect in Fructose intolerance syndrome and in galactosemia (page

139)

12. Why do diabetic patients(blood glucose is high) have problems with their eyes

(cataract, retinopathy), or kidneys? Page 140

Gluconeogenesis

1. Why do we need to synthesized glucose de novo?

2. What are precursors of glucose in gluconeogenesis? P 117

3. What is the role of biotin in oxaloacetate formation? (P.118)

4. In animal, can acetyl-CoA be used in gluconeogenesis, if not, why/ if yes how?

5. Name 3 unique gluconeogenesis reactions and 4 enzymes.

6. Why liver but not muscle is the major organs to generate glucose into bloodsteam

7. What are two organs that can release free glucose into blood stream: Why? Where is the

enzyme glucose 6 phosphatase located? Glycogen storage disease typeIq

Page 121

8. After a meal 2,6 bisphosphate is high because …….. is released and make

enzyme………in a Phospho/dephospho form and inactive/active . Page 121

Pentose phosphate pathway

1. Why do animal cells need to do glucose oxidation? (P. 145)

2. What is the functional difference between NADH and NADPH?

3. How do cells synthesize other carbon numbered sugar from hexose such as ribose and what

is the role of thiamine pyrophosphate here? ( page 147)

4. Why does G6PD cause haemolysis in some certain conditions? (P. 152-3)

5. What are uses of NADPH? (P147 -155)

Glycogen synthesis and degradation

1. Tell amount of glycogen in muscle and liver? Which organ has more glycogen/weight?

Which organs in our body supply blood glucose?

2. What is glycogenin? P 127

3. During eating or right after meal , what enzyme in glycogen metabolism should be

activated and in which form and by what hormone? and which is inactivate?

4. How is α 1,6 glycosidic bond of glycogen formed and broken down? (P. 127-8)

5. What is the role of UDP glucose pyrophosphorylase in glycogen synthesis?

26

6. What enzyme deficiency in Glycogen storage disease that shows symptom of execise

intolerance, with no rise in blood lactate during exercise.( p 129)

7. Epinehrine and glucacon have the same effect of hepatic glycogen metabolism ? What form

of glycogen synthase would it be ? phosphorylate / dephosphorylate and is it active or not

active?

8. Why does glycogen break down generate glucose-1-phosphate without using ATP and how

does the product change to glucose-6-phosphate

9. Why do most glycogen storage diseases cause hepatomegaly (enlarge liver)


2. Q&A 10 min.


References: Lehninger: Chapter 14, 15 (2 Chapters only),


27

LESSON PLAN

Small Group Conference 1: Active Learning Lesson: Molecular Technology in Medicine

Conference Coordinator: Laran T. Jensen, Biochemistry, Faculty of Science

Date/Time: Monday, 18 September 2017, 9.30-10.30

Room: SC1-161

Learning Objectives: 1. To let students gain more knowledge by fortifying from unknown or uncertain to better

understanding with chalenging activities

2. To indirectly train students to be punctual and good willing to participate the lesson

3. To be able to gather crucial information and construct concepts and plans of management

Content Outlines: 1. Molecular mechanisms underlying PCR and hybridization.

2. High-throughput DNA sequencing.

3. Personalized genome/Individualized Medicine.

4. Genetic engineering

Learning Organization: 1. Introduction to the activity.

2. Bingo game

3. Compare and contrast.

4. Case study questions.

5. Mind mapping

Learning Materials Provided: 1. Sildes and Bingo table

2. Blank Tables to be filled in

3. A case study and paper for mind mapping

Student Assessment: 10% of total score per conference

• Attendance and punctuality 3%

• Answering in the activity 3%

• Mind mapping (by Group) 4%

Reading Materials: 1. Lehninger Principles of Biochemistry (4th edition)

2. http://www.pyrosequencing.com/DynPage.aspx?id=7454

3. Culliton BJ (1976) Recombinant DNA: Cambridge City Council votes moratorium. Science

193(4250):300-1.

28

LESSON PLAN

Laboratory 2: Enzyme LDH

Lab Coordinator: Kittisak Yokthongwattana, Biochemistry, Faculty of Science

Date/Time: Tuesday 18 September 2017, 13.30-16.30

Room: SC3-lab

Learning Objectives: Student should be able to

1. measure enzyme activity that is a specific property of enzyme.

2. calculate the the Km and Vmax values that are the characteristic of each enzyme.

3. explain the isoenzymes efficiency in different organs using the Km and Vmax values.

Content Outlines: 1. Determination of bovine late dehydrogenase (H4) enzyme activity

2. Determination of Km and Vmax of the LDH (H4) by Lineweave-Burk plot


2. Lab preview 30 min, OP-ชัชวาล.









3. Voet, D., and Voet, J. G., Biochemistry, John Wiley & Sons, New York, 1990.

Student Assessment: For processes evaluation: 5% of total score per lab

• Quiz or pre-test and Attendance 30%



29

LESSON PLAN

Lecture 10: Citric Acid Cycle and Oxidative Phosphorylation

Instructor: Tuangporn Suthiphongchai, Biochemistry, Faculty of Science

Date/Time: Monday 25 Sept 2017, 9.30-11.30

Room: SC1-161


Student will be able to

1. Introduction to metabolism

1.1. discuss thermodynamic functions (ΔG) and the meaning of spontaneous change and

equilibrium.

1.2. explain free energy change upon ATP hydrolysis and role of ATP as energy currency.

1.3. discuss the concept of high energy biomolecules and their roles in coupled reactions

and other biological processes.

1.4. explain the concept of oxidation-reduction reaction, half reactions, reduction potential

and the use of coenzymes as electron carriers in biological system.

1.5. recognize the importance of flow of electron in the redox reaction to provide energy for

doing biological work.

1.6. define catabolism and anabolism.

2. Fate of pyruvate, citric acid cycle, electron transport and oxidative phosphorylation

2.1. describe fates of the pyruvate under aerobic and anaerobic conditions.

2.2. outline citric acid cycle (TCA or Krebs’ cycle) and discuss its function in the oxidation of

acetate and production of electrons.

2.3. explain the process of electron transfer in mitochrondria to regenerate of oxidized

coenzyme and to produce proton gradient from energy of this electron transfer.

2.4. discuss the coupling in oxidative phosphorylation (role of ATP synthase in

transformation of energy from proton gradient into ATP synthesis).

2.5. compare and contrast oxidative phosphorylation and substrate level phosphorylation.

2.6. discuss the effects of uncouplers and electron transport inhibitors.

30

Lecture Outlines: 1. Introduction to metabolism

1.1. Therodynamics, concepts of equilibrium, Gibbs free energy, and energy transformation

in biological systems

1.2. Phosphoryl group transfers, role of ATP and coupling reaction

1.3. Oxidation-reduction reactions:- half-reaction, reduction potential, biological redox

reaction, flow of electron in biological work, coenzymes as electron carriers

1.4. Energy metabolism: anabolism/catabolism

2. Fate of pyruvate, citric acid cycle, electron transport and oxidative phosphorylation

2.1. Fate of pyruvate in aerobic and anaerobic conditions

2.2. Citric acid cycle:- oxidation of acetate to carbon dioxide, electron production

2.3. Regulation of citric acid cycle; by allosteric property of pyruvate dehydrogenase

complex, and three exogonic steps

2.4. The importance of intermediates in citric acid cycle in anabolism

2.5. Electron transfer in mitochrondria: component in electron transport chain, regeneration

of oxidized coenzyme and electron flow, inhibitors

2.6. Coupling of electron transport and oxidative phosphorylation: proton gradient, ATP

synthase,

2.7. Effects of uncouplers and electron transport inhibitors

Leading questions: Fate of pyruvate

1. In anaerobic condition or insufficient of O2 to be used in tissue, what is the fate of

pyruvate, why does it happen that way and how do tissues reuse it when O2

consumption becomes sufficient? (P. 538)

2. What is the role of a derivative of vitamin B1, thiamine pyrophosphate, in formation of

acetyl-CoA? (P. 540-541)

Citric acid cycle

1. What are the three major stages of cellular respiration? (P 601)

2. Pyruvate dehydrogenase complex is a cluster of three enzymes and five cofactors.

What types of reaction does it catalyse? Write down the overall reaction and explain

the function of each cofactor. (P 602 and P 605 or summary 16.1 P 606)

3. What is the net reaction of citric acid cycle? How many GTP and reduced electron

carriers are produced from 1 acetyl CoA? In which organelle does the reaction occur?

(P 607)

4. Write down the following reactions in the citric acid cycle:- condensation,

decarboxylation, oxidation reduction and substrate-level phosphorylation reactions,

What are the forms of energy produced from this complete oxidation of acetyl CoA. (P

606-607)

5. Intermediates in the citric acid cycle can be used for anabolic pathway. How these

intermediated are replenished? (P 616-618) What is/are the role(s) of biotin in those

processes? (P 618)

6. Can intermediates in citric acid cycle such as Succinyl CoA be used to synthesis

glucose? How? (P 617, Fig 16-15; P 543-544, P548)

7. How is citric acid cycle regulated? (P621, 16.3 first paragraph; and P 623, Summary)

31

Electron transport chain and Oxidative phosphorylation

1. In electron transport chain what is the terminal electron acceptor molecule and what is

the final product? (P 690)

2. What are the differences between oxidative phosphorylation and substrate level

phosphorylation (P 690, P 531)

3. Write down the series of electron transfer starting from NADH to the terminal electron

acceptor. How does this order of electron transfer related to the redox potential of

each electron carrier? (P 694-696)

4. Where is the complex I to IV localized? What are their functions in electron transport

chain? (P 696)

5. Concerning electron transport chain, what is “Proton gradient” or “Electrochemical

potential”? Where does the gradient occur in animal cell? How does electron transfer

generate proton gradient? What is its significance? (P 701)

6. In oxidative phosphorylation, how is ATP synthesized? What is the energy driving the

synthesis of ATP? (P 704-707)

7. What does “Coupling” in oxidative phosphorylation refer to? (P 704-705 Fig 19-18)

8. What is “Respiratory uncoupler” Give one example of uncoupler and its mechanism of

action (p705, p707)

9. Why is cyanide or carbonmonoxide highly toxic? (P 696 fig 19-6, P 705)

10. How can DNP lead to overheat production in the cell? (P 705, P 707)


2. Q&A 10 min.


References: 1. Lehninger Principle of Biochemistry 4th edition, 2005

Part II Bioenergetics and Metabolism (P.481-488)

Chapter 15 Principles of Bioenergetics

Chapter 16 The Citric Acid Cycle

Chapter 19 Oxidative Phosphorylation

2. multimedia in

http://www.wiley.com/legacy/college/boyer/0470003790/animations/animations.htm

:Citric acid cycle and Cori cycle

3. http://cbag2.sc.mahidol.ac.th/bc_intranet/th/course_schdule/SCID221/index.php

:ATP synthase (Ed Wood)


32

LESSON PLAN

Small Group Conference 2: Hemoglobin Structure and Functions

Conference Coordinator: Kittisak Yokthongwattana, Biochemistry, Faculty of Science

Date/Time: Tuesday, 26 September 2017, 13.30-15.30

Room: SC1-161

Learning Objectives:Students will be able to

1. discuss their understanding of hemoglobin structure how it functions

2. integrate and understand basic concepts learned from Lecture 1 - 4 on structure and

function relationship of biomolecules

3. apply basic physical concept to understand biochemical processes

Learning Materials: Part 1

• Conference questions are assigned to students.

• Each students study the assigned question and present their answer in front of the class

Part 2

• Students are assigned a post test to quiz their understanding of the material of the

conference and the tutorial 1 and 2

Reference: • Lehninger Principles of Biochemistry by Nelson and Cox, 4th Edition 2005 page 157 - 174

Conference Content:

Hemoglobin is one of many molecules that comprise erythrocytes (red blood cells) and give them

their ability to bind and transport oxygen to and from the many different tissues of the body. In this

part of the conference, we will discuss structurally how hemoglobin performs its function.

Questions:

1. Compare and contrast the structure of hemoglobin and myoglobin. What are the differences and

similarities between the two proteins in terms of structure and function?

2. Discuss the cooperative binding of oxygen by hemoglobin A. What are the T state and R state?

3. Explain how CO2 is transported from tissues to lung.

4. What is the Bohr Effect? How is it related to the T and R states of the hemoglobin?

5. CO2 transport by the red blood cell in tissues is usually accompanied by a change in pH. The pH

change can affect the amino acid side chains in protein differently due to different in individual’s

pKa value(s). Explain the meaning of pKa.

6. Histidine is an amino acid with 3 pKa values of 2, 6 and 9, respectively. What is the net charge of

histidine at pH 1.5, 5, 7, and 10?

33

7. Explain how BPG is involved in human adaptation to high altitude.

8. During early development, the human fetus expresses different α and β hemoglobin genes. These

are similar but not identical to the hemoglobin genes expressed in adults. This fetal hemoglobin is

less sensitive to BPG than the adult hemoglobin. As a result, fetal hemoglobin has a higher affinity

for oxygen, allowing transfer from the maternal adult hemoglobin. The structural difference

between the fetal and adult hemoglobin is that the amino acid residue 143 of the β chain in adult

hemoglobin is histidine while that of the fetal hemoglobin is serine. Discuss how this single amino

acid difference contributes to different sensitivity to BPG.

9. What is the effect of each of the following treatments on the oxygen affinity of hemoglobin A?

(a) Increase pH from 7.2 – 7.4

(b) Increase pCO2 from 10 – 40 torrs

(c) Increase concentration of BPG from 2x10-4 – 8x10

-4 M

(d) Dissociation of α2β2 into monomeric subunits

10. Explain how sickle-cell anemia is caused. What goes wrong with the hemoglobin of patient with

such disease?

34

LESSON PLAN

Lecture 11: Amino Acids Metabolism


Date/Time: Monday, 2 October 2017, 8.30-10.30

Room: SC1-161


1. describe overall nitrogen metabolism

2. describe how dietary proteins are digested and transported

3. describe metabolic fate of amino groups

4. explain urea cycle, its control and its role in the nitrogen excretion.The role of special

enzymes glutamine synthetase and glutamate dehydrogenase in the nitrogen preservation

in our body.

5. discuss pathways of amino acid degradation (in general)

6. describe some diseases causing by defects in amino acid metabolism

7. explain how we can synthesize some amino acids (non essentials)

and important molecules that derived from them

Content Outline: 1. Amino acid pool, protein turn over : 2. Digestion of dietary proteins: proteolytic enzymes in GT tract, pancreatic proteases.

Transport into cells (intestine and kidney).

3. Metabolic fate of amino groups: transamination, oxidative deamination , transportation of

ammonia to hepatic tissues , liver disease marker

4. urea cycle: reactions, krebs bicycle, urea cycle regulation, genetic defect in urea cycle

enzymes, ammonia metabolism, hyperammonemia

5. Amino acid degradation: ketogenic vs glucogenic amino acid, vitamin and cofactors

involved.

6. Some genetic disorders (metabolic diseases) affecting amino acid catabolism.

7. Amino acid biosynthesis (essential vs non essential )

8. Molecules derived from amino acid.

Leading Questions:1. Draw transamination reaction of 4 amino acids commonly found in metabolism.

2. What is the role of vitamin B6 in the amino acid metabolism?

3. Explain the link between urea and Kreb’s cycle, list enzymes and coumpounds in urea cycle,

Draw overall stoichiometry of the urea cycle? P254-6

4. What is the waste composition in urea molecule and where do these molecule come from?

Why it is dangerous if intake only protein diet and vitamins to lose weight?

5. Why certain amino acid should be restricted in diabetic patient? List amino acid that are

glucogenic, or ketogenic or both. (P. 262)

6. What are the functions of Alanine transaminase (ALT) and aspartate transaminase (AST)?

What are the roles of these two enzyme as diagnostic tool? Liver has larger amount of

which enzyme p. 251

7. Why some amino acids are considered to be essential and what are they ?(p267-8

8. Some genetic diseases in amino acid metabolism are quite unique and occasionally appear

such as albinism, phenylketouria, alkaptouria, maple syrup urine disease and

35

argininosuccinic academia.homocystinuria Which defective enzymes are they, what are

accumulated intermediates , treatment if any? P269

9. What are sources of ammonia ? Is ammonia toxic:? What are symptoms. Two major causes

of hyperammonemia ? Which urea cycle enzyme that is x-linked genetic inherited and most

commonly found of these disorder? P257-8

10.What is Methyl malonyl CoA acidimia? How it is related to amino acid degradation?

11.List cofactor/coenzyme involve in one carbon transfer? How it is related to amino acid

/nucleotide metabolism? p 264,267

12.Which amino acid is the precursor of these substances: dopamine, adrenaline,

norepinehprine, tyroxine, glutathione, porphyrin, GABA, histamine, nitric oxide?


2. Q&A 10 min.


Learning Materials Provided: • Slides from PowerPoint lecture presentation

References: • Chapters 21-22 of Nelson, D. L., and Cox, M. M., Lehninger Principles of Biochemistry, 4th

edition, W. H. Freeman and Company, New York, 2005 or comparable chapters in other text

books.


36

LESSON PLAN

Lecture 12: Nutrition and vitamins



Room: SC1-161

Learning Objectives:Students should be able to

1. define dietary refence intakes

2. describe energy requirement in human, energy from food and macronutrients distribution

ranges including carbohydrate , fat , protein.

3. list some major health problems that can be related to unhealthy food intake, eating

disorders (bulimia, anorexia nervosa, obesity, under nutrition).

4. recognize vitamins structures and explain their functions and derivatives of medical

important requirements, deficiency and/or toxicities.

5. list micronutrients minerals, their deficiency and toxicities

Content outline:1. Dietary reference intake: estimated Average requirement(EAR) recommended dietary

allowance(RDA), upper intake level(UL)

2. Nutrients: 6 classes of nutrients, macro and micro nutrients and their functions

3. Energy balance: calories needed per day related to nutrients

4. Vitamins structure and functions, their toxicities, and deficiency symptoms: water soluble

and fat soluble vitamins

5. Minerals: major vs. trace elements : their functions and deficiency symptoms

6. Health problems related to unhealthy food intake

Leading Questions(373-93)

1. What is the differences between EAR and RDA?Which one is more popular to use and why?

2. What are acceptable macronutrient distribution range ? for carbohydrate, lipid and

proteing? (361) Is carbohydrate is fattening food ?

3. Give example of food that have low glycemic index. What are they good for?

4. What is trans fatty acid? What kind of food generate it? What is omega 3 and omega 6 fatty

acid? What are their benefit (362-3)

5. What determine quality of protein? (p367) List Protein Energy malnutrition(PEM)(page 369)

6. Which of the vitamins would most likely become deficient in a vegetarian person?

7. What are the structures of the vitamin B1 ,B6 and B12 and their active form ?What are

their deficiency symptoms? What are reactions or enzymes they involve in?

8. What is the function of vitamin K in relation to blood clotting?

9. What is WERNICKE-KORSAKOFF SYNDROME?

10. List two major enzymes that have vitamin B12 as coenzyme? (375)

11. Describe relationship of vitamin B6 B12 and folate in methionine metabolism and

homocysteine blood level.

12.A Thai infant presents with prominent forehead, bowing of the limbs, broad and tender

wrists, and irritability. Which of the vitamins is recommended?

13. A 55-year-old woman has fatigue for a long time. Blood studies reveal a macrocytic anema,

homocysteine level is elevated but not methylmalonic acid. Which of the vitamin should she be

prescribed?

Is it true that taking calcium supplement during menopause will increase bone mass and

prevent osteoporosis?

37

14. If an animal was given only vitamin A in the form of vitamin A acid only since born, What kind

of symptoms or condition that this animal should develop?

15. What kind of reaction types or enzymes that vitamin B6 act as coenzyme? List at least 4 (378)

17. What s the difference pernicious anemia and megaloblastic anemia? (377)

18. Vitamin B1 is coenzyme for oxidative decarboxylation of three substrates. Please list and related

to the symptoms of Beri beri.

19. Eating only corn as a staple food can cause pellagra. Please explain.

20. What vitamin can be used to treat hyperlipidemia?

21. What symptoms may happen in people who have only high protein diet and not fruit and

vegetables ?


2. Q&A 10 min.

Reference:• Baynes, J.W. and Dominiczak, M.H., Medical Biochemistry, 2nd edition, Elsevier 2005


38

LESSON PLAN

PBL: Hunger Strike

Scenario Organizers: Jamorn Somana, Biochemistry, Faculty of Science

Tutors: Jamorn Somana, Tuangporn Suthiphongchai Biochemistry, Faculty of Science

Date/Time: 1st Meeting: Tuesday, 3 October 2017, 13:30-15:30

2nd Meeting: Monday, 7 November 2017, 13:30-15:30

Room: SC1-161 and one more room

Learning Objectives:Students should be able to use the active learning method to

1. describe the effect of food deprivation on metabolism and discuss the mechanisms by which

the body attempts to maintain blood glucose level.

2. appreciate the concepts of metabolic specialization and fuel preferences of individual

tissues.

3. discuss the processes involved in nitrogen homeostasis.

4. discuss the critical role of ketone bodies during starvation.

5. describe the consequences of prolonged deficiency of micronutrients.

Learning Outlines:A case scenario of a man on hunger strike, brought to a hospital by his wife. Problems, medical

history, physical examination and laboratory investigation are included.

Learning Organization:1. A scenario is provided at least one week in advance to the students and tutors.

2. A written tutorial guide on the case is provided in advance to the tutors who will facilitate

the active learning process of the students.

3. Students are divided into 28 groups; each group contains 10-13 students. A tutor is

assigned for each PBL group. Students will have two 2-hr meeting sessions.

4. The first session allows the students to use critical thinking and relevant discussions to

formulate the learning objectives.

5. Students carry out independent study on the assigned learning objectives by using a variety

of information resources.

6. In the second meeting session in the following week, students report their findings to the

group, and through exchanging ideas and discussions, formulate the hypothesis and draw

conclusion.

Learning Materials:1. A case scenario.

2. Textbooks and material resources relevant to the problem.

Assessment: by students and tutors

1. Performance (identifying, solving problems, active learning and presentation).

2. PBL test at the end of the course.

39

Learning Organization: • Lecture

• Questions and answers




books.


40

LESSON PLAN

Lecture 7: Nucleotide Metabolism

Instructor: Tuangporn Suthiphongchai, Biochemistry Faculty of Science

Date/Time: Monday 9 October 2017, 9.30-11.30

Room: SC1-161

Learning objectives:

The student should be able to

1. explain 2 distinct biosynthesis pathways of purines and pyrimidines (de novo and salvage

pathway).

2. explain the degradation pathway of purine and pyrimidine nucleotides.

3. list some diseases caused by metabolic disorder of purine and pyrimidine metabolism.

4. explain how purines and pyrimidines metabolic pathway can be used to develop

chemotherapeutic agents.

Content outlines:1. Biosynthesis of nucleotides and its regulation: de novo: purines (862-66) pyrimidines (866-

72), salvage pathway (875)

2. Degradation of purines and pyrimidines (873-75)

3. Diseases caused by defect in nucleotide biosynthesis and degradation pathway, i.e. gout,

lesh-nyhan, ADA deficiency (873-5)

4. Chemotherapeutic drug target in thymidylate and folate metabolism (876-77)

Leading Questions:1. What are the differences between de novo and salvage pathway biosynthesis of

nucleotides?

2. What amino acid can be precursor in de novo synthesis of both purines and pyrimidines?

3. How deoxyribonucleotides are made from ribonucleotides? What are the roles of thioredoxin

and glutathione in these reactions(869-71)

4. How does one carbon group transfer from one compound to another and how does it link to

methionine, cysteine synthesis, vitamin B12 and folic? (P. 672-674, 845)

5. What are functions of ribonucleotide in the cell beside the building box of RNA?

6. What is the reason to have methyl group for dTMP in DNA but not for UMP in RNA?

7. What are differences between de novo and salvage pathway?

8. How does human body excrete and control amount of uric? (P. 874-875)

9. How different between gout and Lesch Nyhan syndrome? (P. 875)

10.Why some food such as poultry, entrails, young vegetable shoot and fermented food are

not suitable for gout patients?

11.Allopurinol is a drug to treat gout, what is the mechanism of this compound?(876)

12.We normally don’t degrade nucleotides to produce energy as compare to carbohydrate, fat

and protein? What evidence or observations should you think it would be?

13.List anticancer drugs that target enzymes involving in nucleotides metabolism

14.What the differences between Gout and Lesh Nyhan syndrome? Why Lesh Nyhan syndrome

patients also develop gout or hyperuricimia?

41


2. Q&A 10 min.





books.


42

LESSON PLAN

Tutorial 1: Q&A Structure & Function, Gene regulation & DNA technology

Tutorial Staffs: Laran, Kittisak, Biochemistry, Faculty of Science

Date/Time: Tuesday, 10 October 2017, 13.30-15.30

Room: SC2-203


1. raise questions regarding the lecture topics not understood to tutorial instructors.

2. spend the time in the tutorial to clarify lecture contents.

Learning organization: 1. Students study the learning materials in advance according to the outline content and

questions for students to answer after they study the content.

2. Students post any questions regarding the tutorial content prior to or at the tutorial session.

3. Questions are answered and explained at the tutorial session.

43

LESSON PLAN

Small Group Conference 3: Active Learning Lesson: Diabetes

Conference Coordinator: Jamorn Somana, Biochemistry, Faculty of Science


Room: SC1-161

Learning Objectives: To let students gain more knowledge by fortifying from unknown or uncertain to better

understanding with chalenging activities

To indirectly train students to be punctual and good willing to participate the lesson

To be able to gather crucial information and construct concepts and plans of management

Content Outlines: 1. General facts about Diabetes

2. Differences of clinical manifestration, blood and hormorns changes in each type of diabetes

in some certain conditions

3. A case scinario with some typical problems of diabetes

Learning Organization: 1. Introduction to the activity.

2. Bingo game

3. Compare and contrast.

4. Case study questions.

5. Mind mapping

Learning Materials Provided: 1. Sildes and Bingo table

2. Blank Tables to be filled in

3. A case study and paper for mind mapping

Student Assessment: 10% of total score per conference

• Attendance and punctuality 3%

• Answering in the activity 3%

• Mind mapping (by Group) 4%

44

LESSON PLAN

Lecture 14: Lipid Metabolism

Instructor: Jamorn Somana, Biochemistry, Faculty of Science


Room: SC1-161

Learning Objectives: Student will be able to

1. explain digestion, mobilization and transport of fats.

2. describe utilization and storage of energy in lipid form, generation of ATP from fatty acids

and ketone bodies

3. identify similarities and differences between fatty acid oxidation and fatty acid synthesis and

control of fatty acid oxidation and biosynthesis

Content Outlines:1. Absorption and transportation of dietary fat in the body and lipoproteins

2. Regulation of fatty acid oxidation and biosynthesis

4. Ketone bodies generation and usage

5. Essential fatty acid and ecosanoid compounds which are linked to NSAIDs

Leading QuestionsFatty acid catabolism

• Why lipid (triglyceride) is more suitable as storage fuels compare to carbohydrate? (P.173)

• How does lipid transport from intestine to target tissues? How do apolipoproteins and

lipase involve in this process? (P. 228-229)

• What is the effect of epinephrine on lipid metabolism in adipose tissue? (P.190)

• What is the role of carnitine and coenzyme A in fatty acid degradation? (P.191)

• What is the rate limiting step (regulatory step) in fatty acid oxidation? (P.190-191)

• Write down four repeated reactions of beta-oxidation and their products. (P.192 Fig 16.17)

• How do human oxidize cis form of unsaturated fatty acid? (Lehninger P.637-639 Fig 17-

8&17-9)

• What is the function of Acyl CoA dehydrogenase? What would be the effect of Acyl CoA

deficiency? (P.192-193)

• Besides normal coenzymes required for general beta-oxidation, what are

coenzymes/cofactors required for oxidation of odd-number fatty acid? What are their

functions? (P.195 fig 16-20)

• What are ketone bodies and how do they generated? (P.195-197 fig 16-22-16.25)

Lipid biosynthesis

• How does biosynthesis of fatty acids differ from their breakdown? (P. 183-187)

• How is malonyl-CoA involved in fatty acid biosynthesis? (P.183 fig. 16.9)

• What is the coenzyme help in catalyzing carboxylation reaction by acting as CO2 carrier and

transfer CO2 to organic substrate? (P.119 fig. 10.3)

• Which is the first fatty acid formed by the fatty acid biosynthesis process and how it is

formed? (P. 185 fig.16.9)

• Where is the fatty acid biosynthesis taken place? How does the substrate for this process

transported to that site? (P.185-187 fig. 16.11)

45

• What is the source (form) of electron used for reduction reactions in fatty acid biosynthesis?

(P. 146, 185 fig.13.2, 16.9)

• What is the rate limiting step for fatty acid synthesis? (P. 184, fig. 16.7)

• How insulin, glucagon and fatty acyl CoA level regulate fatty acid biosynthesis? (P. 184, fig.

16.8)

• Can mammalian cells synthesize polyunsaturated fatty acids such as linolenic acid? Why are

polyunsaturated fatty acids necessary for our body? (P.213-215 fig.17.21-17.25)

• Fatty acids are substrates for synthesis of variety of signaling molecules in a family of

eicosanoids such as prostaglandins, thromboxane, leucotrienes. What are the fatty acid

substrate and the key enzymes for synthesis these compounds? (P.215)

• What is the role of certain drugs like aspirin and ibuprofen? (P. 216)

• What are the common processes in the biosynthesis of both triacylglycerols and

glycerophospholipids? (P. 203)

• How is heart disease related to cholesterol, how it is initiated? (P. 236-237 fig. 18.22)

• What are VLDL, LDL, HDL and chylomicron? How do they differ from one another? (P. 227-

232 fig. 18.13-18.19)

• How do cells get rid of plasma LDL particles? (P. 233)

• Many drugs for treatment of hypercholesterolemia, such as lovastatin, act on inhibiting

cholesterol synthesis by inhibiting enzyme at the rate-limiting step. What is the rate-limiting

step in the synthesis of cholesterol? How hormone and cholesterol level regulate

cholesterol synthesis? (P.220-224 fig. 18.3-18.8)


2. Q&A 10 min.


References:• Lippincott’s Illustrated Reviews Biochemistry, 6

th edtion

• Lehninger Principle of Biochemistry 4th edition, 2005


46

LESSON PLAN

Lecture 15: Heme and Minerals Metabolism



Room: SC1-161


1. describe how heme is synthesized, degraded and eliminated from the body.

2. dxplain some clinical conditions which are connected to abnormal heme metabolism.

3. describe the special chemical properties of some minerals in biochemical reactions.

4. explain how the body take up, maintain and modify some minerals.

Content Outlines: 1. Tetrapyrrole synthesis for heme and its degradation

2. Porphyria and hyperbillirubinemia

3. Special chemical properties of some minerals such as Fe, Co, Cu, P, S and I.

4. Biochemical reactions and metabolic pathways which link to some minerals

Leading Questions:Heme Metabolism

1. What are precursors and the first committed intermediate of porphyrins synthesis? (P. 855)

2. What is the significant difference in term of structure between preuroporphyrinogen

(uroporphyrinogen I) and uroporphyrinogen III? (P. 855)

3. Why many pyrrole compounds are phototoxic?

4. What is the function of haem in haemoproteins? (P. 158, 693)

5. Why does high level of haemolysis cause jaundice and how does the body cope with this

condition? (P. 856)

6. Why our serum urine and feces have yellowish-brown colour? Do those colours come from

the same compound? (P. 856)

7. What is enterohepatic circulation?

8. Why do many porphyrias coincide with anemia? (P.857)

Mineral Metabolism

1. Why is calcium deposited in the bone?

2. What are the roles of phosphate in biomolecules?

3. How iron is able to carry oxygen in hemoglobin or transfer electron in cytochromes.

4. What is the special property of cobalt in methylmalonyl-CoA mutase?

5. What is Wilson disease? How does it link to copper metabolism?

6. What are roles of Zinc in enzyme catalysis and complexing with some proteins and DNA?

7. What are the roles of sulfur compounds in carbohydrate and protein structures?

8. Why does iodine need to be cation before integrated into tyroxine?

47

LESSON PLAN

Laboratory 3: Determination of Serum lipid

Lab Coordinator: Jamorn, Biochemistry, Faculty of Science


Room: SC3-lab

Learning Objectives: Student should be able

1. To familiarize biochemical and enzymatic assays for determination of triglyceride and

cholesterol

2. To be able to evaluate serum lipid status and correlate to clinical interpretation

Content Outlines: 1. Determine serum total cholesterol

2. Determine serum total triglycerides

3. From the provided HDL-cholesterol values determine LDL-cholesterol

4. Calculate atherogenic index


2. Lab preview 30 min, OP-ชัชวาล.









3. Allain CC et al. Enzymatic determination of total serum cholesterol. Clin Chem. 1974; 20:

470-475.

4. Mgowan MW et al. A peroxidase couple method for the colorimetric determination of serum

triglycerides. Clin Chem. 1983; 29: 538-542.

5. Friedewald WT. Estimation of concentration of low-density lipoprotein cholesterol in plasma,

without use of the preparative ultracentrifuge, Cli Chem. 1972; 18: 499-502.

6. Gill PI et al. Regulation of acyl CoA: Cholesterol acyl transferase activity in normal and

atherotic aortas: Role of a cholesterol substrate pool. Exp Mol pathol. 1986; 44: 320-329.

Student Assessment: For processes evaluation: 5% of total score per lab

• Quiz or pre-test or Attendance 30%



48

LESSON PLAN

Lecture 16: Integration and Regulation of Metabolism

Instructors: Jamorn Somana, Biochemistry, Faculty of Science

Date/Time: Monday, 6 November 2017, 9.30-11.30

Room: SC1-161

Learning Objectives: Students will be able to understand metabolism and functions, hormones functions and

mechanisms, hormones and control of metabolism, regulations of metabolism, metabolic

integration in the coordinated and orderly functions of the organs, and the physiological

biochemistry on body functions.

Content Outlines:1. Metabolism

1.1 The physiological or integrated and precise practical concept on the functions of

metabolism.

1.2 Metabolism and the metabolic pathways localization or compartmentalization in cells

and tissues (organs).

1.3 Bioenergetics and metabolism, the relationship of catabolic and anabolic processes in

cell (organ) functions.

1.4 Oxidation-reduction reactions in the production of energy, what about the associated

free radicals?

1.5 Monitoring techniques (MRI and NMR) for the metabolic events in different organs, the

powerful medical approaches on metabolism as relevance to diagnosis and prognosis.

1.6 Clinical aspects of metabolic processes, the importance on balance of metabolism and

corrections for the deficiency or the excess of certain specific metabolites.

2. Hormones Functions and Mechanisms

2.1 Types of Hormones based on their structures, from small molecules to macromolecules

(proteins).

2.2 Hormones classification based on the functions and mechanisms of the actions.

2.3 Hydrophobic (lipophilic) and hydrophilic, another way in viewing the types of

hormones.

2.4 Anabolic and the catabolic hormones, the protagonist and antagonist (Yin-Yang) of the

hormone controls.

2.5 Medical endocrinology, hormones and analogs (drugs) in the control for the orderly and

coordinated functions of the cells, tissues and the organs (body functions).

3. Hormones and Control of Metabolism

3.1 Transcriptional control and the post-translational control of enzymes by hormones in

metabolic pathways regulation.

3.2 Feedback loop of hormone levels control in the regulation of metabolic processes.

3.3 Communication of the metabolic pathways and the balanced level of hormones, cross-

talk or feedback control by the key metabolites (intermediates) and/or the products

(i.e. glucose) in the regulation of hormone levels.

3.4 Balanced metabolic processes (or Homeostasis) by hormones and the coordinated

orderly organ functions.

49

3.5 Abnormality of hormones (level) and the abnormality or dysfunction of certain specific

metabolic processes.


2. Q&A 10 min.


References: Lehninger Principles of Biochemistry; Nelson and Cox, 4th Edition, 2005. (Good standard

text and very informative for good backgrounds, but maybe a bit too detailed for readings?)

50

LESSON PLAN

Lecture 17: Biochemistry knowledge and medicine



Room: SC1-161

Learning ObjectivesStudents will be able to

1. Describe some basic biochemistry knowledge in medical applications

2. Understanding of some changing in biochemistry parameters with disease status

Content Outline 1. Explanation of basic blood biochemistry values

2. Effect of some physiological changes to biochemical compounds in the body

3. Some diseases with some specific biochemical features

4. Some nutrition imbalances and pathogenesis via abnormal biochemistry

5. Enzyme kinetic with therapeutic applications

6. Some applications of DNA technology

Learning OrganizationStudying the learning materials provided in advance

1. Lecture 100 min

2. Questions and answers 20 min

Learning Materials Provided 1. Slides from PowerPoint lecture presentation

ReferencesNelson, D. L., and Cox, M. M., Lehninger Principles of Biochemistry, 4

th edition, W. H.

Freeman and Company, New York, 2005 or comparable chapters in other text books.

Student AssessmentMCQ Exam

51

LESSON PLAN

Tutorial 2: Q&A Metabolism, Medical Application

Tutorial Staffs: Jamorn, Tuangporn, Wilai, Biochemistry, Faculty of Science


Room: SC1-161


1. raise questions regarding the lecture topics not understood to tutorial instructors.

2. spend the time in the tutorial to clarify lecture contents on metabolic pathways.

Learning organization: 1. Students study the learning materials in advance according to the outline content and

questions for students to answer after they study the content.

2. Students post any questions regarding the tutorial content prior to or at the tutorial session.

3. Questions are answered and explained at the tutorial session.

52

Teaching team of SCBM 281-282First semester, Academic year 2017

Teaching StaffAssoc. Prof. Dr. Laran T. Jensen

Assoc. Prof. Dr. Kittisak Yokthongwattana

Assoc. Prof. Dr. Tuangporn Suthiphongchai

Assoc. Prof. Dr. Wilai Noonpakdee

Assist. Prof. Dr. Jamorn Somana

Teaching Assistant

CoordinatorAssist. Prof. Dr. Jamorn Somana

Ms. Rattanavinan Hanchaina

53

Student ID Name Lab group PBL group5905547 SCBM/B Miss Nattawan Wilertsak 1 15905549 SCBM/B Miss Thanyalak Ganjiang 2 25905550 SCBM/B Miss Binte Zainab 3 15905551 SCBM/B Mr. Prathomphong Yeo 4 25905552 SCBM/B Miss Plydaow Po-ngern 5 15905553 SCBM/B Miss Pimchanok Panpinyaporn 6 25905554 SCBM/B Miss Piraya Chaiyo 7 15905555 SCBM/B Miss Peeraya Sukcharoenchaikul 8 25905556 SCBM/B Miss Paradee Unchaleevilawan 9 15905557 SCBM/B Miss Muratha Sottatipreedawong 10 25905560 SCBM/B Mr. Wanchalerm Yenjai 1 15905561 SCBM/B Mr. Vichaya Truskamol 2 25905562 SCBM/B Miss Sarinya Sirivisitakul 3 15905563 SCBM/B Miss Samita Boonpitak 4 25905567 SCBM/B Mr. Abdul Waris azizi 5 15905568 SCBM/B Mr. Ethan James booth 6 25905632 SCBM/B Miss Krishna Gajera 7 15905634 SCBM/B Mr. Chonchanut Lasort 8 25905636 SCBM/B Miss Yanika Dubey 9 15905638 SCBM/B Miss Nichakorn Nookeaw 10 25905639 SCBM/B Mr. Torlarp Sitthiwanit 1 15905643 SCBM/B Miss Benyapa Lertritdecha 2 25905644 SCBM/B Miss Pariyaporn Sombunsuko 3 15905645 SCBM/B Miss Puniga Chansara 4 25905646 SCBM/B Miss Pattaraporn Thaworasak 5 15905649 SCBM/B Miss Monsicha Natpotchananon 6 25905650 SCBM/B Miss Methawee Nateechaisit 7 15905652 SCBM/B Mr. Wasin Samutpradit 8 25905654 SCBM/B Mr. Sittichoke Chaowalit 9 15805535 SCBE/B Miss Nontaroth Kanil 10 25805536 SCBE/B Miss Puntaree Pratuang 1 1

Documents

Academic Year 2017: 21 August 2017 – 27 November 2017 ... · 3 Course Syllabus and Lesson Plan SCBM 282 Medical Biochemistry Laboratory: From Molecules to Cells (Chemical processes