Hb and Mb
What is the quaternary structure of
Myoglobin?
Hemoglobin?
None or monomer
Tetramer (2 alpha and 2 beta)
Enzymes will affect this (1) to speed up the rate of the reaction but it will NOT affect this! (2)
(1) Activation Energy
(2) Delta G of the reaction
His E7
What does His F8, Val E11 and Phe CD1 do?
This is the apoenzyme plus it's cofactor
The Holoenzyme (Think "W"hole enzyme)
Hydrogen and bicarb will bind to these things that make the T stat "tense"
H-Bonds and Ion pairs only present in the T State
This DIPF will inhibit what?
ALL serine proteases including: Chymotrypsin/Trypsin/Elastase and Thrombin, AChe and anything that has the catalytic triad with a serine in it's active site
At a high pH the hemoglobin in your body will favor this state.
R State (high pH = low H+ concentration less of an inhibitor means the protein is active)
Bonus questions where does the H bind?
Describe the Serine Protease Mechanism
1) GABC via His 57
2) Covalent Ca. (Ser 195)
3) Electrostatic stabilization (Asp 102 and the 2 backbone amid NH's)
Be very familiar with this and prepared to answer several MCQ's on the exam about this very important mechanism.
The hill coefficients below mean this:
3?
.4?
0?
Positive cooperative (ex. Hemoglobin)
Negative cooperative
Non-cooperative (Ex. Myoglobin)
What are the EC classification numbers and what do they each mean?
EC Numbers:
1 - Oxidoreductase
2 - Transferase
3 - Hydrolase
4- Lyase
5 - Isomerase
6 - Ligase