Hemoglobin Structure and Function Flashcards

1
Q

Hemoglobinopathies

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

Hemoglobin vs. Myoglobin

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

3 Demensional Folding of Myoglobin

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

What is a Heme Group?

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

Heme oxidation States and binding

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

Oxygen binding to heme

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

Carbon Monoxide Binding to Heme without Distal Histidine

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

Carbon Monoxide Binding to Heme with Distal Histidine

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

Comparision of CO and O2 Binding to Myoglobin

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

Tertiary/Quaternary Structure of Hemoglobin

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

Features of Quaternary Structure

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

Cooperativity as a series of Equilibria

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

Comparision of Oxygen Binding Curves of Rstate and Tstate

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

What are the major regulators of Cooperative Oxygen Binding

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

Hemoglobin and Allosteric Sturcutre Function Relationship

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Key Residues of Beta Chain Involved in the Allosteric Mechanism of Cooperativity

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Interactions of the Deoxy T form

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Hemoglobin Key Beta Chain Residues

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

The Globin Pocket

A
20
Q

Hemoglobin Conformational Changes

A
21
Q

Space Filling Model of Hb Oxygenation

A
22
Q

Comparision of Oxygen Binding Curves for Myoglobin and Hemoglobin

A
23
Q

Oxygen Binding of Fetal Hemoglobin

A
24
Q

Relevant Features of 2,3 BPG

A
25
Q

BPG Binding to Hemoglobin

A
26
Q

Rotation of the Alpha Beta Dimer

A
27
Q

Allosteric Effects of BPG

A
28
Q

How does cooperativity occur?

A
29
Q

Iron interaction with Oxygen in tense and relaxed states

A
30
Q

Mechanism of the Tense to Relaxed Form

A
31
Q

Heme role in modulating protein structure

A
32
Q

Molecular Basis for Hemoglobin Cooperativity

A
33
Q

A Mechanism for Oxygen Binding

A
34
Q

A mechanism for Oxygen Binding Cont.

A
35
Q

The Bohr Effect

A
36
Q

Effect of CO2 on O2 affinity of Hemoglobin

A
37
Q

Effect of Allosteric Effectors on the Oxygen Affinity for Hemoglobin

A
38
Q

Role of His 146 in Bohr Effect

A
39
Q

CO2 transported in the blood from tissue to lungs

A
40
Q

Influence of Bohr Effect on Carbonic Acid and CO2 equlibrium

A
41
Q

Summary of Mechanism of Coorperativity

A
42
Q

HbS Sickle Cell Disease

A
43
Q

Amino Acid Alteration in Sickle Cell

A
44
Q

Aggregation and Polymerization of HbS

A
45
Q

Sickle Cell Disease Biochemical Defect

A