Lectures 1-10

Question 1

Peptide bond

Answer 1

bond between amino acids

Question 2

Primary structure

Answer 2

linear

Question 3

secondary structure

Answer 3

how linear folds upon itself helix, alpha and beta

Question 4

tertiary

Answer 4

distant interaction

Question 5

quartenary

Answer 5

bond between multiple peptides dimer, trimer, tetramer–> eg: hemoglobin is tetramer

Question 6

polypeptide

Answer 6

amino acids linked together

Question 7

rate enhancement

Answer 7

effect of lowering the activation energy

Question 8

how enzymes function

Answer 8

bring two things together and make them react. Lowering the activation energy

Question 9

four catalytic mechanisms

Answer 9

-acid-base catalysis -Metal-ion cofactors -entropy reduction -covalent intermediates

Question 10

N-terminal

Answer 10

the end of a polypeptide that has an amino

Question 11

C-terminal

Answer 11

the end of a polypeptide that has a carboxyl group

Question 12

relationship between Ea and rate of rxn

Answer 12

As Ea decreases, rate increases

Question 13

Binding Isotherm

Answer 13

equation that shows concentrations of ligands to binding sites as [L] increases or decreases

has a rectangular hyperbola graph

Question 14

Binding isotherm equation

Answer 14

L_B=(L/L + K_d) * B

LB= concentration of L bound to B

k_d= strength of interaction between L & B. The lower k_d=better binding

B= [protein]

Question 15

K_d of ligand binding

Answer 15

dissociation constant, shows he [L] needed to reach 50% of saturation

“fit” of ligand indicatior, lower is better

Question 16

high affinity/ low affinity

Answer 16

two states of a tetramer,

Question 17

cooperativity

Answer 17

when the concentration of a ligand alters the binding properties of the protein

Question 18

Michaelis-Menton Equation

Answer 18