Session 11 ILO's Protein Function and Regulation Flashcards

1
Q

List the major regulatory mechanisms that control enzyme activity (plus examples)

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Discuss the allosteric properties of a key regulatory enzyme

what is allostery?
R and T states allosteric effectors give examples

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Discuss the concept of enzyme cascades and the use of protein kinases and phosphatases to regulate activity

why cascades are important
what is a kinase/phosphatase?
why does phosphorylation have an effect?

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Define the term zymogen (with examples).

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Explain how activation of the clotting cascade leads to the formation of fibrin

NOT a detailed description of clotting process

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Discuss the mechanisms that are involved in the regulation of clot formation and breakdown

focus on the regulation of the process
types of regulatory mechanisms involved
clotting as an example of a highly regulated process

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Explain the physiological roles of myoglobin and haemoglobin

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Contrast the oxygen-binding properties of myoglobin and haemoglobin and explain why haemoglobin is most suited to its role as an oxygen transporter

Molecular features of O2 binding to globins
Why is the oxygen binding curve for myoglobin hyperbolic? Why is the oxygen binding curve for haemoglobin sigmoidal?
- binding and release of oxygen

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Describe the major structural differences between oxygenated and deoxygenated haemoglobin and the molecular basis of cooperativity

T state – low affinity for oxygen

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Describe the effects of CO2, H+, 2,3-bisphosphoglycerate and carbon monoxide on the binding of oxygen by haemoglobin, and the physiological significance of these effects

activators shift curve to the left and enhance high affinity R state inhibitors shift the curve to the right and enhance the low affinity T state

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Appreciate that mutations in globin genes can give rise to diseases such as sickle cell anaemia

molecular basis for sickle cell anaemia

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Outline of the key features needed for protein secretion

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Describe the differences between constitutive and regulated secretion

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Outline of the structure of collagen

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Outline of the processing of collagen

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly