Lecture 8: PROTEINS IN ACTION - 2 Flashcards
What does deoxyhaemoglobin have?
A dished haem
What does oxygen in oxyhemoglobin do?
Flatten the haem and pulls histidine F8 and helix F towards the binding site (increasing its binding affinity for oxygen)
What weakens oxygen binding?
Anything that keeps helix F away
What does the oxygen in oxyhemoglobin do to the fe2+?
Moves it into the plane of the haem, draws His F8 down and repositions the helix F
What are shifts in protein secondary elements called?
Conformation changes
What is an example of the conformational change?
Helix F moving relative to helix c
Where is the most change observed?
At the FG loop
What happens to side chain packing in R and T states?
The interaction between side chains of the F helix and C helix change
Positions of side chains in R and T states are both …
stable
The transition state between R and T is …
Unstable so not much time is spent in that position
Describe the changes when going from R to T conformation?
The F helix moves so that the interaction between threonine and aspartic acid is borked and an interaction with a different threonine and asparagine is formed. This makes the binding pocket larger
What is BPG?
2,3-bisphosphoglycerate
What is BPG?
An allosteric inhibitor of oxygen binding to haemoglobin
What is the charge of BPG?
Highly negatively charged
How does BPG bind to deoxyhaemoglobin?
By electrostatic interaction
What does BPG do?
Stabilises haemoglobin in the deoxygenated T state, reducing oxygen affintiy