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Lec 2 Flashcards

1
Q

What is hemeprotien ?

A

Polypeptide chain with heme group

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2
Q

What is the role of heme group in cytochrome & catalase & hemoglobin?

A

Cytochrome: electron carrier
Catalase : catalyze the breakdown of hydrogen peroxide
Hemoglobin:bind to oxygen

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3
Q

Heme structure ?

A

Protoporphyrin IX and FE in the center

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4
Q

Myoglobin consist of how many polypeptide chain ?

A

1

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6
Q

One polypeptide of hemoglobin or myoglobin consist of how many alpha helical structure?

A

8 , A B C D E F G H

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7
Q

Which bond stabilizing alpha helix of myoglobin polypeptide?

A

Hydrogen bond & ionic bond

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8
Q

Interior of myoglobin consist of ?

A

Non polar amino acid which make hydrophobic bond to packed and stabilize the structure

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9
Q

Surface of myoglobin consist of ?

A

Polar amino acid which stabilize the structure by hydrogen bond

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10
Q

Proximal histidine occurs at ?

A

F alpha helix and bind directly to FE

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11
Q

Distal histidine occurs at ?

A

E alpha helix and bind to oxygen which bind to Fe (indirect)

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12
Q

What is the main role of hemoglobin?

A

Transport oxygen

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13
Q

How many oxygen cal hemoglobin transport?

A

Four

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14
Q

What is the interaction between alpha & beta in the dimmer ?

A

Hydrophobic

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15
Q

What is the interaction between two dimmers?

A

Hydrogen & ionic bond

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16
Q

T form of hemoglobin is deoxy or oxy hemoglobin?

A

Deoxyhemoglobin

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17
Q

How many oxygen does T form of hemoglobin carried ?

A

Zeroooo

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18
Q

In any form there are many hydrogen bond?

A

T form

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19
Q

Which form of hemoglobin have higher affinity to oxygen and which one have lower?

A

R form have higher and T form have lower

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20
Q

What is the change that occurs after bind oxygen to hemoglobin ?

A

Interdimer interaction or ionic & hydrogen bond will broken which lead to more free movement of polypeptide chane

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21
Q

Hitch one have high affinity to oxygen ? Hemoglobin or myoglobin?

A

Myoglobin

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22
Q

What is the shape of dissociation curve of myoglobin?

A

Hyperbolic shape

23
Q

What is the shape of dissociation curve of hemoglobin?

A

Sigmoid also shape

24
Q

Why hemoglobin make sigmoidal dissociation curve ?

A

Due to allosteric effect

25
Q

What is the allosteric effect

A

Binding of one oxygen to hemoglobin increase hemoglobin affinity to other atoms of oxygen

26
Which molecules of oxygen is more difficult to bind to hemoglobin ? And which one have the easiest one ?
First one have the difficult and last one have the easiest due to allosteric effect
27
Increased metabolites lead to shift curve to ? And why
Shift to right because increase co2 , acidity, temperature and 2,3-BPG which lead to decrease affinity to oxygen
28
2,3-BPG bind to detox or oxy hemoglobin?
Deoxyhemoglobin
29
2,3-BPG decreased or increased affinity of oxygen ?
Decreased and shift curve to right
30
Where 2,3BPG bind on hemoglobin?
On beta chain , on positive amino acid such as histidine & lysine because it have negative charge
31
In pregnancy, the affinity of oxygen increased or decreased?
Decreased because increased 2,3-BPG about 30%
32
Which hemoglobin have higher affinity to oxygen?Hb A or HB F? And y
HB F because it doesn’t affected by 2,3-BPG
33
HB F shift curve to ?
Leeeeeeft
34
Met HB & co HB shift curve to ?
Leeeeft
35
HB A2 consist of ? And when it appears
2 alpha & 2 delta , and appears after 12 weeks(3month) of birth
36
HB A2 increase in thalassemia or sickle cell anemia?
It increased in thalassemia and still normal on sickle cell anemia
37
Which type of HB use to measure blood glucose?
HB A1c
38
What is hemoglobinopathies?
group of disorders passed down through families (inherited) in which there is abnormal production or structure of the hemoglobin molecule
39
What is fatal hemoglobin?
This occurs when HB F fall to convert to HB A | Fall gamma to convert to beta
40
What is sickle cell anemia?
Point mutation in gene for beta globin
41
Any type of anemia produced by sickle cell anemia?
Hemolytic anemia (destruction of red blood cell)
42
What is the abnormal amino acid in sickle cell anima?
Valine which get place glutamate
43
Whcich one has more negativity? HB A / HB S / HB C ? And why ?
HB A because glutamate have negative charge where as valine is neutral (HB S) and lysin have positive charge (HB C)
44
What is HB C ?
Hemoglobin which glutamate in position 6 replaced by lysine
45
Any type of anemia does HB C have ?
Hemolytic anemia
46
Beta thalassemia minor ?
Defective of one gene that produced beta globin (heterozygous)
47
Cooley anemia?
Beta thalassemia major , which have defer in two beta gene (which produced beta globin)
48
Beta thalassemia?
Mutation in chromosome number 11 , in beta gene which lead to insufficient beta globin
49
Alpha thalassemia ?
Defect on chromosome 16 , alpha gene , which lead to insufficient alpha chain
50
What is HB H ?
Hemoglobin consist of 4 beta chain , this result from alpha thalassemia when 3 gene of alpha get mutation and this cause moderate hemolytic anemia
51
What is HB Bart?
Hemoglobin consist of 4 chain of gamma , this produced due to alpha thalassemia in which 4 alpha gene get mutation
52
What is primaquine drugs ?
This drug use to kill malaria , this drugs mustn’t be used in patients with G6PD deficiency
53
Which two of alpha helix bound with FE ?
F bind directly by histidine amino acid , E indirectly by bind to oxygen and oxygen bind to Fe

Biochem HLS (3 decks)

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