Exam 1 Part 5

Question 1

How to get enzyme and substrates together

Answer 1

Diffusion
Scaffolding
Limiting space of diffusion
Activation of proximal proteins

Question 2

Michaelis-Menton equation

Answer 2

V=Vmax[S]/Km +[S]

Question 3

Competitive inhibition

Answer 3

inhibitant and substrate both bind to active site

Question 4

noncompetitive inhibition

Answer 4

inhibitant and substrate bind to different sites on the enzyme

Question 5

allosteric regulation

Answer 5

regulation of an enzyme with a molecule that is not the substrate or product - binds to another site (noncompetitive)

Question 6

Committed step

Answer 6

step that has many input factors in an enzymatic reaction. Energy favorable/saving of energy to regulate at this step

Question 7

allosteric inhibition

Answer 7

enzyme is active in the uncomplexed form, which has a high affinity for its substrate. an allosteric inhibitor stabilizes the enzyme in its low affinity form

Question 8

allosteric actiivation

Answer 8

an enzyme in its uncomplexed form and therefore has low affinity for its substrate. An allosteric activator stabilizes the enzyme in the high affinity form

Question 9

irreversible inhibitors

Answer 9

covalently bound (nerve gases, penicillin, aspirin) can be done in cells as well - phosphorylation

Question 10

reversible inhibitors

Answer 10

can bind a dissociate

non-covalent

Question 11

protein functions

Answer 11

enzymes, motor proteins, receptors, structural proteins, storage, gene regulation, transport proteins, signaling proteins, etc

Question 12

protein formation

Answer 12

form by polymerization of amino acids

Question 13

protein cues for folding

Answer 13

chemical interactions between side chains or backbone will be the cues for folding

Question 14

primary structure

Answer 14

amino acid sequence

Question 15

secondary structure

Answer 15

backbone interactions

Question 16

tertiary structure

Answer 16

3D and R group interactions within 1 polypeptide chain

Question 17

quaternary structure

Answer 17

multiple polypeptide chains

Question 18

What happens when a substrate binds

Answer 18

binds weakly to R group components
Distortion of bonds
enzyme accepts or donates protons, changing reactivity of a substrate (pH)
accepts or donates elections (forming of high E covalent bonds
stabilizes unstable bonds

Question 19

electrophoresis analysis

Answer 19

need to make a negative charge and denature proteins so that they separate by size

Question 20

Things needed for eletrophoresis

Answer 20

gel matrix (polyacrylamide)
buffer
denaturing agents (beta-ME, heat)
anionic detergent (SDS)

Question 21

SDS-PAGE

Answer 21

Sodium dodecyl sulfate polyacrylamide gel electrophoresis

Question 22

things to do after SDS-PAGE

Answer 22

stain and visualize the sizes and amounts of proteins present
-transfer proteins to a membrane and probe for specific proteins
-elute proteins off gel and ID with mass spec
enzymatic reactions in gel