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MCB 181R Sec 3/4H
(August 24 September 16)
The Science of Biology
Review of Chemistry
Organic Chemistry Macromolecules
Cells
Functions of Cell Membranes Review for Exam 1
Exam 1 -- Study Sessions 1-6 (September 16)
1
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(polynucleotides)
2
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Polymers are made by condensation (dehydration)
reactions and broken down by hydrolysis.
3
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Todaywe will consider the four classes oflarge
(macro) molecules found in allliving things.
Proteins provide structure, catalysis, regulation,movement, transport, and recognition in cells.
Polysaccharides are used for energy storage and
building materials.
Nucleic Acids store and transmit hereditary
information.
Lipids are diverse hydrophobic molecules which
function as hormones (steroids), as part of
biological membranes (phospholipids) and in
energy storage (fats).
4
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Proteins provide structure, catalysis, regulation,
movement, transport, and recognition in cells.
Aprotein consists of one or more polypeptide
chains folded into a specific conformation (shape).
Apolypeptide is a long chain or polymer of amino
acids connected in a specific sequence.
The information that specifies the sequences of
amino acids in the thousands of different kinds of
proteins in cells is stored in genes (DNA ofchromosomes).
5
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Cells build proteins with 20 different amino acids!
All amino acids have an
amino and a carboxyl
group linked to an alpha
() carbon atom.
The 20 different amino
acids have the same
general structure but
have different R groups(side chains) that impart
unique characteristics.
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In neutral conditions (pH 7), the amino and carboxyl
groups ionize to NH3+ and COO, respectively
this helps amino acids stay in solution and makes
them more reactive.
7
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The twenty amino acids of proteins are grouped
according to chemical properties of the side chain!
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(hydrophobic)
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*
(hydrophylic)
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*has a special role
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(hydrophylic)
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A protein (one or more polypeptides) consists of
amino acids linked together by peptide bonds!
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Within the polypeptide, the peptide bonds form a backbone with threekey characteristics:
R-group orientation: Side chains can interact with each other or water.
Directionality: Free amino group, on the left, is called the N-terminus.
Free carboxyl group, on the right, is called the C-terminus.
Flexibility: Single bonds on either side of the peptide bond can rotate,making the entire structure flexible.
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A functional protein has up to four levels of structure:
Primary and Secondary structures
Primary structure refersto the sequence or order
of the 20 different amino
acids in the polypeptide
chain.
As a result of hydrogen
bonding, the polypeptide
can coil ( helix) or fold
(-pleated sheet) to give
the secondary structure.
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Tertiary structure
Polar, nonpolar and ionic side chains of the variousamino acids can interact to superimpose a threedimensional shape on the polypeptide referred to asthe tertiary structure.
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A functional protein has up to four levels of
structure!
Polar, nonpolar and ionic side chains of the variousamino acids can interact to superimpose a threedimensional shape on the polypeptide referred to asthe tertiary structure.
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Hydrophobic and van der Waals interactions within
proteins
Hydrophobic Interactions: interactions of nonpolar Rgroups within protein in the presence of a polar
solvent (water). Hydrophobic side chains tend to form
globular masses. Weaker than hydrogen bonds.
van der Waals Interactions: interactions of electrons
of nonpolar R groups within protein. Weakest type of
interactions. But a large number of van der Waals
interactions tend to occur within a polypeptide withmany hydrophobic residues. Many interactions add
up to a significant increase in stability of the
polypeptide.
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A functional protein has up to four levels of structure!
Quaternary structure isthe overall protein
structure resulting from
aggregation of more than
one polypeptide. The
hemoglobin protein in
human red blood cells
consists of four
polypeptides.
20
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Primary Structure: Amino acid monomers are joined,
Figure 3.7 The Four Levels ofProtein Structure
Amino acid monomers Peptide bond
forming polypeptide chains.
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Figure 3.7 The Four Levels ofProtein Structure
Secondary Structure: Polypeptide chains may form a helices
-Helix
Hydrogen bond
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Figure 3.7 The Four Levels ofProtein Structure
-Pleated sheet
or -pleated sheets.
Hydrogen bond
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Figure 3.7 The Four Levels ofProtein Structure
Tertiary Structure: Polypeptides fold, forming specific shapes.
Folds are stabilized by bonds and disulfide bridges.
-Pleated sheet
-Helix
Hydrogen bond
Disulfide bridge
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Figure 3.7 The Four Levels ofProtein Structure
Quaternary Structure: Twoor more polypeptides assemble to form larger protein
molecules. The hypothetical molecule here is a tetramer, made up of four polypeptide
subunits.
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One-minute-break slide!
My office hours:Tues & Thurs 1-2 pm
Wed 9-11 am
or by appointment.Location: Marley 441D
27
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Todaywe will consider the four classes oflarge
(macro) molecules found in allliving things.
Proteins provide structure, catalysis, regulation,movement, transport, and recognition in cells.
Polysaccharides are used for energy storage and
building materials.
Nucleic Acids store and transmit hereditary
information.
Lipids are diverse hydrophobic molecules which
function as hormones (steroids), as part of
biological membranes (phospholipids) and in
energy storage (fats).
28
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Polysaccharides (carbohydrates) are used for
energy storage and building materials.
Apolysaccharide consists of a long chain orpolymer of monosaccharides (simple sugars) such
as glucose.
Cells make polysaccharides by using catalyticproteins called enzymes which perform a
condensation (dehydration) reaction to link simple
sugars together.
Polysaccharides are carbohydrates that contain
carbon, hydrogen and oxygen in the proportion
CH2O.
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Sugars exist inlinear and ring forms
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Monosaccharides Are Simple Sugars
These hexoseshave the same
molecular formulaas glucose(C6H12O6), but theyhave a differentarrangement ofatoms resulting inisomerswithdifferent
properties.
Glyceraldehyde isthe smallestmonosaccharideand exists only as alinear-chain form. Ribose and
deoxyribose eachhave five carbons,but they have verydifferent chemicalproperties andbiological roles.
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Cells build polysaccharides bylinking
monosaccharides together by a glycosidic bond!
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Cellulose, starch and glycogen are all
polysaccharides made of glucose!
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Cellulose, starch and glycogen are all
polysaccharides made of glucose!
35
Plant cellwall Starch granules in plant
cells
Glycogen deposits in
humanliver
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Todaywe will consider the four classes oflarge
(macro) molecules found in allliving things.
Proteins provide structure, catalysis, regulation,movement, transport, and recognition in cells.
Polysaccharides are used for energy storage and
building materials.
Nucleic Acids store and transmit hereditary
information.
Lipids are diverse hydrophobic molecules which
function as hormones (steroids), as part of
biological membranes (phospholipids) and in
energy storage (fats).
36
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Nucleic acids store and transmit hereditary
information!
Nucleic acids consists of a long chain or polymer
of nucleotides.
There are two types of nucleic acids:Deoxyribonucleic Acid (DNA) and Ribonucleic Acid
(RNA)
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A nucleotide consist of a nitrogen-containing base,
a pentose sugar and one or more phosphate
groups!
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Nucleotides are joined by a dehydration
(condensation) reaction to form a phosphodiester
linkage.
39
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The sugar-phosphatebackbone of a nucleic acidis directionalone end hasan unlinked 5carbon, andthe other end has anunlinked 3carbon.
The nucleotide sequence iswritten in the 5p 3direction. This reflects thesequence in whichnucleotides are added to agrowing molecule.
This nucleotide sequencecomprises the nucleic acidsprimary structure.
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A DNA molecule consists of two polynucleotide strands held
together by hydrogen bonds between the nitrogenous
bases!
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The secondary structure ofDNA is a double helix.
42http://www.youtube.com/watch?v=ZGHkHMoyC5I
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Todaywe will consider the four classes oflarge
(macro) molecules found in allliving things.
Proteins provide structure, catalysis, regulation,movement, transport, and recognition in cells.
Polysaccharides are used for energy storage and
building materials.
Nucleic Acids store and transmit hereditary
information.
Lipids are diverse hydrophobic molecules which
function as hormones (steroids), as part of
biological membranes (phospholipids) and in
energy storage (fats).
43
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Fats store large amounts of energy!
Fats (triglycerides) are made from two kinds of molecules (glycerol and
fatty acids) by a condensation (dehydration reaction).
44
These fatty acid chains
can have different
hydrocarbon chain
length or structure,
some saturated and
some unsaturated.
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Fatty acids vary inlength and they may be saturated or
unsaturated!
Saturated fatty acids: nodouble bonds betweencarbonsit is saturatedwith H atoms.
Unsaturated fatty acids:some double bonds incarbon chain.
monounsaturated: one
double bond
polyunsaturated: morethan one
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Phospholipids are building blocks of cell membranes!
Phospholipids have 2rather than 3 fatty acidswith a phosphate group onthe third position on theglycerol molecule.
Additionally, small chargedor polar molecules (e.g.choline) are linked to thephosphate group.
The resulting phospholipid
is amphipathic with bothhydrophobic andhydrophilic portion of themolecule.
47
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Phospholipids spontaneously form a bilayer
structure inwater
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Phospholipids spontaneously form a bilayer structure inwater with their hydrophobic hydrocarbon tailsclustered together and the polar phosphate head
groups associated with water molecules.
49
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Lipid bilayers show selective permeability
50
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S id li id h l f
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Steroids are lipids that regulate many aspects of
growth! Steroids are characterized by a carbon skeleton consisting of four fused
rings. Cholesterol is a common component of human cell membranes and is
essential for synthesis of other sterols.
Sex hormones like testosterone are made from cholesterol.
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Bonds, bonds and more bonds!
Covalent shared pair of electrons
Ionic electrostatic attraction between anions and cations
Hydrogen attraction between hydrogen and oxygen ornitrogen
Peptide links amino acids together in polypeptides
Disulfide bond between two S atoms stabilizing tertiarystructure of polypeptides
Ester linkage between fatty acids and glycerol oftriglycerides
Glycosidic linkage between sugars in polysaccharides
Phosphodiester linkage between nucleotides inpolynucleotides (DNA and RNA)
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