Exam2

Question 1

Given structures, figure out which structure has all atoms in a plane?

Answer 1

C-N-C structure

Question 2

Given 4 equations,

What is Ka1/Ka2
O2+Heme–free–> Ka1
CO+Heme–free–>Ka2

Answer 2

5x10^-5

1/20,000 = 5x10^-5

Question 3

Definition for

Motif, Subunit, Domain

Answer 3

Motif: Supersecondary structure; collection of secondary structures

Domains: Globular units/proteins

Subunit: secondary protein

Question 4

Parkinsons, Mad Cow are a product of what

Answer 4

Protein folding defects

Question 5

Which is FALSE

Answer 5

Collagen is RIGHT hand helix and LEFT hand superhelix

Question 6

What is kd value of P1Mc1 - protease

Answer 6

2.0 x 10 ^-8

Question 7

Given [L] and [P]
30% of bind sites ocupied

Increase [L] to X what is new % of binding sites occupied?

Answer 7

50%

theta=[L]/([L]+Kd)

Question 8

Myoglobin bind __ O2 and Hemoglobin bind __ O2

Answer 8

Mb: 1
Hb:4

Question 9

What is not true of BPG

Answer 9

It is negative heterotropic regulator

Question 10

What is true of hemoglobin affinity for O2

Answer 10

Affinity of Hb for O2 in lungs at sea level is greater than its affinity in peripheral tissues at 4500M

Question 11

What statement is correct

Answer 11

H+ decrease the affinity of Hb for O2 by binding in different site in Hb

Question 12

Which statement is correct #2

Answer 12

Hb(a) + Hb(b) + Mb are only 20% same, but 3D structure remarkably similar

Question 13

Apoenzyme?

Answer 13

(apoprotein) is without Mg++ or Enzyme alone (no group!)

Question 14

Cooperative Energy

Answer 14

Curve looks like the one on chapter 5 slide no 18 one on the middle J

Question 15

Enzyme increase rate of reaction by

Answer 15

More than 100%

Question 16

Reaction Energy Curve

Answer 16

Look and do
Binding Energy
Activation energy
Change in Delta G (80Kj/mol)

Question 17

Amino acid with guanidinum group

Answer 17

Arginine

Question 18

“Induced Fit” involved in the reaction catalyzed by _____ and the normal substrate of this reaction is _____

Answer 18

Hexokinase and Glucose

Question 19

What is following reaction from graph?

Answer 19

Acid-Base and Metal Ion Catalysis

Question 20

What is true about enzyme kinetic

Answer 20

At the saturation level, the enzyme catalytic activity is direction proportional to the enzyme concentration

Question 21

Inhibitor binds to a site other than the Active Site of Enzyme-Substrate Complex

Answer 21

Uncompetitive

Question 22

Inhibitor binds to a site other than the Active Site of the Enzyme alone or of the Enzyme-Substrate complex

Answer 22

Mixed

Question 23

Enzyme conc. -- 1 uM
Substrate conc #1 -- 200 uM 
Vo = 98.1
Substrate conc #2: 500uM
Vo= 99.1

Enzyme conc is now 2uM what is Vmax

Answer 23

200

Question 24

Enzyme conc. = 1uM
Km= 20
What will Vmax be at Km=40

Answer 24

Answer is 67

Question 25

What is the Kcat from Q25

Answer 25

Answer was 100 min-1

Question 26

From this graph you should be able to answer Km and Vmax

Answer 26

Km = 1/.05=20
Vmax= 1/0.1= 10

Question 27

From table should be able to answer Km and types of inhibitors

Answer 27

In case of Z (0.0005) and Absence of inhibitor (0.0002)

Question 28

Which can bind to the enzyme Before or After substrate binding

Answer 28

Mixed and Uncompetitive

Question 29

Which type of inhibition curve is this

Answer 29

Competitive Inhibition

Question 30

Which is true

Answer 30

Penicillin bind with Beta-Lactamase, molecule separates leaving Active Beta-lact and Inactive penicillin

Question 31

You have reaction pathway with S-T-R-G-W the X catalyst enzyme. What is most likely happening

Answer 31

Substrate W is more likely a negative modulator and has an inhibition feedback effect

Question 32

What is a false statement

Answer 32

Heterotropic Allosteric is competing with a substrate in the Binding Site

Question 33

Proteolysis does not involve in

Answer 33

Inhibition of pencillin Beta-lactamase

Question 34

Which one is HIV inhibitor

Answer 34

Indavir
Nelfonavir
Lopinavir
Saquinavar