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Chemicals of life
112/04/19 2
The Macromolecules of cells
112/04/19 4
The Unique Water molecule
The water molecule is not linear
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V-shaped linear
Polarity and hydrogen bond
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Polarity and hydrogen bond
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Polarity and hydrogen bond
Result of regular arrangement of water molecules: ice crystals
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Peculiar Properties of water
A waterstrider / pond skater demonstrates how cohesion (H-bonds) between water molecules allow it to move across water's surface.
1. Universal Solvent
2. High heat capacity, heat of fusion, heat of vaporizaton
3. Density & Freezing properties
4. Surface tension
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Water- an universal solvent ----- for polar and charged particles
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Water and oil are immiscible.
“like dissolves like”
oil (long hydrocarbon chain, non-polar)
Vs
water (polar, H-bonding)
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Fatty substances form membrane compartments in cells to allow different reactions to take place independently of one another
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High heat capacity, high heat of vaporization and fusion
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High heat capacity, high heat of vaporization and fusion
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high heat of vaporization
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Cohesion in water molecule
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Cohesion and surface tension
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Cohesion and water transport in plants
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Ice is less dense than water
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What would happen to life in the lake when the lake is frozen?
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Water as a reactant
photosynthesis
digestion
Turgor and wilting Turgor loss in plants causes wilting
Which can be reversed when the plant is watered
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Water- the habitat for many life forms
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Minerals in DNA – P, N,
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Minerals in functional molecules – haemoglobin, chlorophyll
112/04/19 30
Minerals : Iron containing haem in haemoglobin holds oxygen
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Minerals - calcium
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Minerals- nerve activities: ions movements _ Na+, K+
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Carbohydrates
Monosaccharides with different no. of Carbon
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Common Monosaccharides
Six-carbon sugars
Linear and Ring forms
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Alpha and beta form of glucose
Interconversion of Mono-- Di--polysaccharides
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Condensation / dehydration synthesis
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Disaccharides
Reducing and non-reducing sugars
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Test for reducing sugars
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Sugars are sweet! How sweet is it?
SugarRelative sweetness
to sucrose
lactose 0.16
galactose 0.32
maltose 0.33
sucrose 1.0
fructose 1.73
aspartame 180
saccharin 450
Polysaccharide-starch
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helical structure of starch
Starch grains in plant cells
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Mitochondria Glycogen granules
0.5 µm
Glycogen
Glycogen: an animal polysaccharide
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Cellulose- a structural material
LE 5-7
a Glucose
a and b glucose ring structures
b Glucose
Starch: 1–4 linkage of a glucose monomers.
Cellulose: 1–4 linkage of b glucose monomers.
• Polymers with alpha glucose are helical• Polymers with beta glucose are straight• In straight structures, H atoms on one
strand can bond with OH groups on other strands
• Parallel cellulose molecules held together this way are grouped into microfibrils, which form strong building materials for plants
LE 5-8
Cellulosemolecules
Cellulose microfibrilsin a plant cell wall
Cell walls Microfibril
Plant cells
0.5 µm
Glucosemonomer
Enzymes that digest starch by hydrolyzing alpha linkages can’t hydrolyze beta linkages in cellulose
Cellulose in human food passes undigested through the digestive tract as insoluble fiber
Some microbes use enzymes to digest cellulose
Many herbivores, from cows to termites, have symbiotic relationships with these microbes
Chitin, another structural polysaccharide, is found in the exoskeleton of arthropods e.g insects
Chitin also provides structural support for the cell walls of many fungi
Chitin can be used as surgical thread
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Obesity
What are Lipids?
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The unifying feature of lipids is having little or no affinity for water
Lipids are hydrophobic -- becausethey consist mostly of hydrocarbons, which form nonpolar covalent bonds
The most biologically important lipids are fats, phospholipids, and steroids
LE 5-11a
Dehydration reaction in the synthesis of a fatGlycerol
Fatty acid(palmitic acid)
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A Triglyceride
Fats made from saturated fatty acids are called saturated fats
Most animal fats are saturated Saturated fats are solid at room
temperature A diet rich in saturated fats may contribute
to cardiovascular disease through plaque deposits
LE 5-12a
Saturated fat and fatty acid.
Stearic acid
Saturated and unsaturated fats
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Fats made from unsaturated fatty acids are called unsaturated fats
Plant fats and fish fats are usually unsaturated
Plant fats and fish fats are liquid at room temperature and are called oils
LE 5-12b
Unsaturated fat and fatty acid.
Oleic acid
double bondcauses bending
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Phospholipid
-replacing a fatty acid (nonpolar) with a phosphate
(polar)
Phospholipids- lipids with a polar head
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Lipid bilayer
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Lipid bilayer forms membrane
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The basic structure of testosterone (male hormone;睪固酮 ) and estradiol (female hormone;雌激素 ) is identical.
Both are steroids with four fused carbon rings, but they differ in the functional groups attached to the rings.
These then interact with different targets in the body.
Steroid tree
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Proteins have many structures, resulting in a wide range of functions
Proteins account for more than 50% of the dry mass of most cells
Protein functions include support, storage, transport, cellular communications, movement, body defense
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Amino acids – general formula
Variable properties
according to the R group
Amino acids - examples
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Peptide bond - dipeptide
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Amino Acid Polymers
Amino acids are linked by peptide bonds
A polypeptide is a polymer of amino acids
Polypeptides range in length from a few monomers to more than a thousand
Each polypeptide has a unique linear sequence of amino acids
Polypeptides
Polypeptides are polymers of amino acids
A protein consists of one or more polypeptides
Protein Conformation and Function
A functional protein consists of one or more polypeptides folded, and coiled into a unique shape
The sequence of amino acids determines a protein’s three-dimensional conformation
A protein’s conformation determines its function
A ribbon model
Groove
Groove
A space-filling model
Four Levels of Protein Structure
The primary structure of a protein is its unique sequence of amino acids
Secondary structure, found in most proteins, consists of coils and folds in the polypeptide chain
Tertiary structure is determined by interactions among various side chains (R groups)
Quaternary structure results when a protein consists of multiple polypeptide chains
Primary structure, the sequence of amino acids in a protein, is like the order of letters in a long word
Primary structure is determined by inherited genetic information
Typical secondary structures are a coil called a helix and a folded sheet structure
Amino acidsubunits
helix
pleated sheet
Tertiary structure is determined by interactions between R groups, rather than interactions between backbone constituents
These interactions between R groups include hydrogen bonds, ionic bonds, hydrophobic interactions, and van der Waals interactions
Strong covalent bonds called disulfide bridges may reinforce the protein’s conformation
Hydrophobicinteractions andvan der Waalsinteractions
Polypeptidebackbone
Disulfide bridge
Ionic bond
Hydrogenbond
Quaternary structure results when two or more polypeptide chains form one macromolecule
Collagen is a fibrous protein consisting of three polypeptides coiled like a rope
Hemoglobin is a globular protein consisting of four polypeptides: two alpha and two beta chains
Chains
ChainsHemoglobin
IronHeme
CollagenPolypeptide chain
Polypeptidechain
Sickle-Cell Disease: A Simple Change in Primary Structure
A slight change in primary structure can affect a protein’s conformation and ability to function
Sickle-cell disease, an inherited blood disorder, results from a single amino acid substitution in the protein hemoglobin
LE 5-21a
Red bloodcell shape
Normal cells arefull of individualhemoglobinmolecules, eachcarrying oxygen.
10 µm 10 µm
Red bloodcell shape
Fibers of abnormalhemoglobin deformcell into sickleshape.
LE 5-21b
Primarystructure
Secondaryand tertiarystructures
1 2 3
Normal hemoglobin
Val His Leu
4Thr
5Pro
6Glu Glu
7Primarystructure
Secondaryand tertiarystructures
1 2 3
Sickle-cell hemoglobin
Val His Leu
4Thr
5Pro
6Val Glu
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Quaternarystructure
Normalhemoglobin(top view)
Function Molecules donot associatewith oneanother; eachcarries oxygen.
Quaternarystructure
Sickle-cellhemoglobin
Function Molecules interact withone another tocrystallize intoa fiber; capacityto carry oxygenis greatly reduced.
Exposedhydrophobicregion subunit subunit
What Determines Protein Conformation?
In addition to primary structure, physical and chemical conditions can affect conformation
Alternations in pH, salt concentration, temperature, or other environmental factors can cause a protein to unravel
This loss of a protein’s native conformation is called denaturation
A denatured protein is biologically inactive
Protein – internal Forces/ bonding
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LE 5-22
Denaturation
Renaturation
Denatured proteinNormal protein
Protein – What level of protein structure is represented below?
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Protein – Levels of complexity
Protein – globular proteinsproteins with physiological function
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Globular protein e.g. enzyme
Protein – globular proteins: e.g. antibodies
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Structural proteins
Protein – Fibrous proteins with structural function e.g. collagen
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