BIOLOGY 1

January 25, 2017

Biochemistry I

o Four Macromolecules: Protein, Carbohydrates, Lipids, & Nucleic Acids

o Condensation reaction= loses water to form polymers
o Hydrolysis reaction = adds water to break down polymers into monomers

Biological Macromolecules, Protein

o Proteins are synthesized from the N terminus to C terminus
o Primary structure: amino acid sequence
o Secondary structure: interactions between backbone atoms
o Tertiary structure: folding due to side chain interactions
o Quaternary structure: side chain interactions with two or more different peptides
o Proteins function: enzymes, receptors, channels, porters, intra/extra cellular
transport, cell structure, antibodies, hormones, etc.

Biological Macromolecules, Carbohydrates

o Monomer = monosaccharides (glucose, fructose, galactose) Also know: ribose &
deoxyribose
o CxH2xOx
o Polymer= Disaccharide
Maltose glucose + glucose
Sucrose glucose + fructose
Lactose glucose + galactose
o Polymer = Polysaccharides
Glycogen: animal glucose storage
Starch: plant glucose structure
Cellulose: plant structure (humans cant digest)
o Carbohydrate function: cellular energy, cell surface markers, adhesion (unicellular
organisms)

Biological Macromolecules, Lipids

o Monomer = hydrocarbon
o Saturated: containing the greatest possible number of hydrogen atoms (stacks
nicely, normally solid)
o Unsaturated: having carboncarbon double or triple bonds and therefore not
containing the greatest possible number of hydrogen atoms for the number of
carbons.
o Lipids have 4 forms in the body:
Triglyceride: glycerol with three fatty acid molecules (energy storage)
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Phospholipid: amphipathic molecule with a hydrophobic and a hydrophilic

component. (cell membrane)
Terpenes: built from multiple isoprene units (precursor for cholesterol,
steroids)
Cholesterol: 3 six carbon rings and 1 five carbon ring (cell membranes,
steroid precursor)

Thermodynamics and Reaction Coupling

o Gibbs Free Energy =
o G < 0 = spontaneous (exergonic gives energy); G > 0 = nonspontaneous
(endergonic requires energy)
o H = enthalpy (potential stored energy)
o TS = temp x entropy ( kinetic motion energy)

Kinetics and Reaction Coordinate Graph

o Transition state= high energy; unstable
o If activation energy is low reaction proceeds faster (inverse relationship)

Catalysts and Enzymes

o Catalysts increase reaction rate by stabilizing the transition state and reduces
activation energy
o ENZYMES DO NOT AFFECT THERMODYNAMICS
o Enzymes have 3 characteristics:
Must increase rate of reaction
Must not be used up in the reaction
Specific for a particular reaction

Enzyme Structure and Regulation

o Reactants = substrate
o Reaction occurs in the active site
o Enzyme activity is regulated by phosphorylation and allosteric regulation
(alternative binding site)
o Negative feedback/feedback inhibition= ending product forms and inhibits the
enzyme to stop the reaction.
o Positive feedback= ending product forms and enhances reaction to create more
product. (must have external regulator)

V vs. [S] Graph

o 3 different conditions:
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[S] < [E]: At low concentration of substrate, there is a steep increase in the
rate of reaction with increasing substrate concentration. The catalytic site
of the enzyme is empty, waiting for substrate to bind, for much of the
time, and the rate at which product can be formed is limited by the
concentration of substrate which is available.
[S] = [E]: product formation levels off and as the concentration of
substrate increases, the enzyme becomes saturated with substrate. As soon
as the catalytic site is empty, more substrate is available to bind and
undergo reaction. The rate of formation of product now depends on the
activity of the enzyme itself, and adding more substrate will not affect the
rate of the reaction to any significant effect.
[S] > [E]: Vmax reached
o Vmax= The rate of reaction when the enzyme is saturated with substrate is the
maximum rate of reaction.
o Km= the concentration of substrate which permits the enzyme to achieve half
Vmax. (high affinity low Km (not much substrate needed bc good bonding)

Enzyme Inhibition
o Types of Inhibition:
Competitive= binds at active site; Vmax constant; Km increases
Noncompetitive= binds at allosteric site; Vmax decreases; Km constant
Uncompetitive= binds at allosteric site and ES complex; Vmax decreases;
Km decreases
Mixed= binds at allosteric site; Vmax decreases; Km varies

Lineweaver Burk Plots

o Inverse plot: 1/V vs. 1/S