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Lecture 3

BIO270H1 Lecture Notes - Lecture 3: Glycogen Synthase, Beta Sheet, Glycosylation


Department
Biology
Course Code
BIO270H1
Professor
Chris Garside
Lecture
3

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Lecture 3 (September 30, 2015): Biochemical Basis of Psychology Continued
Reading: pg 77-84, 88-90
enzymes can be affected by molecules that are not directly involved in catalysis
competitive inhibition
omolecules compete with substrate for the same active site
okm changes
oif some molecules are bound by an inhibitor, there has to be an increase in
substrate
but it doesn't affect the mass
there is no change in conformation of the enzyme
allosteric activation
omolecules binds to enzyme in a site separate from active site
changes conformation of enzyme which changes how it is bound to the
substrate
lowers the km
can change enzyme kinetics (Vmax)
covalent modification
oby kinase that phosphorylates the enzyme
onegative group changes distribution of charge
ochanges conformation of enzyme
oleads to activation of enzyme and can also be an enzyme repressor
this is dependent on the type of kinase
oprotein phosphotase can remove the phosphate group
Energy Storage
cells store energy in two forms

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oreducing energy
oxidized
ohigh energy molecules
ATP
othe two forms serve as energy currency in the cell
othey drive endergonic reactions (positive free energy)
othey require exergonic reactions to couple with
oprovide energetic support
oact as substrates
Reducing Energy
ocan transfer electrons in redox reactions
ex: NADH, NADPH, FADH2, FMNH2
these determine the redox status
they can carry high energy electrons and transfer them
ooxidoreductases are enzymes that catalyze the transfer from the reductant
(electron donor) to the oxidant (electron acceptor)
olactate dehydrogenase
removes NADH from cytoplasm to allow glycolysis to continue (NADH is
oxidizes to NAD+
Redox Status
oreducing energy within a cell
ocan turn off energy producing pathways
oNADH/NAD+ can drive other reactions
energy can be stored in covalent bonds
oenergy can be released when bonds are hydrolyzed

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exergonic reactions
high energy bonds
when bonds are hydrolyzed, there is a lot of free energy release
ATP is the most versatile high energy molecule
oused in macromolecules synthesis transport
ATP is only produces when it's been used
oex: phosphorylation in muscles can donate a phosphate to ADP to become ATP
BIOMOLECULES
Proteins
contribute to cell structure, function enzymes, cellular processes
have complex 3D structures, coded in DNA, are made of polymers of amino acids
amino acids
omade of an amino group, carboxylic acid, and an R group side chain that is the
distinguishing feature between amino acids
oside chains determine if an amino acid is non polar, polar, charged, hydrophobic,
hydrophilic
othere are 20 amino acids in total
20 amino acids provide extreme diversity in protein structure and function
Structure
oPrimary
linear sequence of amino acids
polypeptide backbone
Nitrogen, Carbon, Carbon, Nitrogen, Carbon, Carbon
oSecondary
alpha helix
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