Exam study guide

Question 1

At the pKA, X percent of structures are protonated.

Answer 1

50%

Question 2

What’s Carbonic Anhydrase’s resting state?

Answer 2

CA-ZnII-OH2+

Question 3

pKa of Zn-H2O in carbonic anhydrase II is ~ X

Answer 3

6.8

Question 4

Which chemical group or groups bind directly to the carbon-containing reaction
substrate when CA is working at pH 5?

Answer 4

Backbone NH and R-OH of Thr 199

Question 5

Which chemical group or groups bind directly to the carbon-containing reaction
substrate when the CA is working at pH 9?

Answer 5

B. Backbone amide NH of Thr 199

Question 6

Which chemical groups bind directly to the carbon-containing reaction product
when the CA is working at pH 9?

Answer 6

Backbone NH and R-OH of Thr 199

Question 7

How do you calculate kcat?

Answer 7

Vmax / [E]total

Question 8

What is KCAT?

Answer 8

rate of product production once bound

Question 9

Higher up, paralell line with Inhibitor means

Answer 9

< Km (increases affinity) by lowering the concentration
of ES. This diminished concentration of ES causes the equilibrium to shift from E +
S to favor the formation of ES.

Question 10

Decreasing Km X affinity

Answer 10

increases

Question 11

Being able to reach VMax, just with a higher concentration of enzyme indicates X inhibitors

Answer 11

Competitive, reversible

Question 12

How to calculate kM

Answer 12

Look at amount of substance for 1/2 vmax

Question 13

parallel lines on a Lineweaver-Burk plot are diagnostic of:

Answer 13

uncompetitive inhibition.

Question 14

Which of the following is most likely to form a liposome?

Answer 14

Glycerophospholipids

Question 15

velocity of a reaction formula

Question 16

multiplicative rule for exponents

Answer 16

add exponents

Question 17

Which ionizable amino acid residues in this network below are thought to be the
source of dissociated protons upon the binding of dioxygen to hemoglobin.

Answer 17

V1, H146