Exam2 Flashcards
Given structures, figure out which structure has all atoms in a plane?
C-N-C structure
Given 4 equations,
What is Ka1/Ka2
O2+Heme–free–> Ka1
CO+Heme–free–>Ka2
5x10^-5
1/20,000 = 5x10^-5
Definition for
Motif, Subunit, Domain
Motif: Supersecondary structure; collection of secondary structures
Domains: Globular units/proteins
Subunit: secondary protein
Parkinsons, Mad Cow are a product of what
Protein folding defects
Which is FALSE
Collagen is RIGHT hand helix and LEFT hand superhelix
What is kd value of P1Mc1 - protease
2.0 x 10 ^-8
Given [L] and [P]
30% of bind sites ocupied
Increase [L] to X what is new % of binding sites occupied?
50%
theta=[L]/([L]+Kd)
Myoglobin bind __ O2 and Hemoglobin bind __ O2
Mb: 1
Hb:4
What is not true of BPG
It is negative heterotropic regulator
What is true of hemoglobin affinity for O2
Affinity of Hb for O2 in lungs at sea level is greater than its affinity in peripheral tissues at 4500M
What statement is correct
H+ decrease the affinity of Hb for O2 by binding in different site in Hb
Which statement is correct #2
Hb(a) + Hb(b) + Mb are only 20% same, but 3D structure remarkably similar
Apoenzyme?
(apoprotein) is without Mg++ or Enzyme alone (no group!)
Cooperative Energy
Curve looks like the one on chapter 5 slide no 18 one on the middle J
Enzyme increase rate of reaction by
More than 100%
Reaction Energy Curve
Look and do
Binding Energy
Activation energy
Change in Delta G (80Kj/mol)
Amino acid with guanidinum group
Arginine
“Induced Fit” involved in the reaction catalyzed by _____ and the normal substrate of this reaction is _____
Hexokinase and Glucose
What is following reaction from graph?
Acid-Base and Metal Ion Catalysis
What is true about enzyme kinetic
At the saturation level, the enzyme catalytic activity is direction proportional to the enzyme concentration
Inhibitor binds to a site other than the Active Site of Enzyme-Substrate Complex
Uncompetitive
Inhibitor binds to a site other than the Active Site of the Enzyme alone or of the Enzyme-Substrate complex
Mixed
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
200
Enzyme conc. = 1uM
Km= 20
What will Vmax be at Km=40
Answer is 67
What is the Kcat from Q25
Answer was 100 min-1
From this graph you should be able to answer Km and Vmax
Km = 1/.05=20 Vmax= 1/0.1= 10
From table should be able to answer Km and types of inhibitors
In case of Z (0.0005) and Absence of inhibitor (0.0002)
Which can bind to the enzyme Before or After substrate binding
Mixed and Uncompetitive
Which type of inhibition curve is this
Competitive Inhibition
Which is true
Penicillin bind with Beta-Lactamase, molecule separates leaving Active Beta-lact and Inactive penicillin
You have reaction pathway with S-T-R-G-W the X catalyst enzyme. What is most likely happening
Substrate W is more likely a negative modulator and has an inhibition feedback effect
What is a false statement
Heterotropic Allosteric is competing with a substrate in the Binding Site
Proteolysis does not involve in
Inhibition of pencillin Beta-lactamase
Which one is HIV inhibitor
Indavir
Nelfonavir
Lopinavir
Saquinavar
