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Biological Chemistry > Structure and Function of Protein > Flashcards

Structure and Function of Protein Flashcards

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1
Q

What do red blood cells do?

A
  • Transfer Oxygen from lungs to tissue

- Transfer Carbon Dioxide from tissue to lungs

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2
Q

Haemoglobin and Myoglobin were the first proteins to:

A
  • Be crystallised - 1849
  • Have mass accurately measured
  • Be studied by ultracentrifugation
  • Be associated with a physiological condition
  • Show that a point mutation can relate to disease
  • Have X-ray structures determined (myoglobin in 1959 -Perutz; Haemoglobin in 1968)
  • Theories of cooperativity and control explain haemoglobin function
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3
Q

Where can the the Backbone structure of Myoglobin be found ?

A

Found in skeletal and heart muscle of vertebrates

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4
Q

What does Myoglobin facilitate ?

A

Myoglobin facilitates rapidly respiring muscle tissue

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5
Q

The rate of O2 diffusion from capillaries to tissue is slow because ?

A

Of the solubility of oxygen

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6
Q

What does Myoglobin increase and facilitates what ?

A

Myoglobin increases the solubility of oxygen. Myoglobin facilitates oxygen diffusion

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7
Q

Explain the Haem complex in myoglobin ?

A

TWO histidine residues anchor the haem (distal and proximal)

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8
Q

What do Globin genes encode ?

A

Haemoglobin

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9
Q

In adults, haemoglobin =

A

Iron containing haem molecules in each of 4 globin proteins: 2 α globins and 2 β globins

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10
Q

During development, different globin genes are expressed which alter ?

A

The oxygen affinity of embryonic and fetal haemoglobin

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11
Q

Where is Haem and Globin synthesis ?

A
  • Haem in mitochondria

- Globin in polyribosomes

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12
Q

What does the mature red blood cell not contain?

A

Mitochondria

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13
Q

Different globins combine with haem to form ?

A

Different haemoglobins

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14
Q

Explain the Eight functional globin chains, arranged in two clusters :

A
  1. β- cluster on the short arm of chromosome 11

2. α - cluster on the short arm of chromosome 16

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15
Q

In order to bind to Oxygen the iron must be ?

A

The iron must be in the Fe(II) for or reduced

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16
Q

What is Fe(III) ?

A

Methemoglobin - can not bind oxygen

17
Q

Protoporphyrin binds O2 to?

A

6th ligand of Fe(II) out of the plane of the haem

18
Q

What is the fifth ligand ?

A

The fifth ligand is a Histidine, F8 on the side across the haem plane.

19
Q

His F8 binds to ?

A

The proximal side

20
Q

What binds to the distal side?

A

Oxygen

21
Q

When haemoglobin is deoxygenated, the heme group adopts a ?

A

Domed configuration

22
Q

When haemoglobin is oxygenated, the haem group adopts a ?

A

Planar configuration

23
Q

The conformational change in the haem group causes?

A

The protein to change its conformation, as well

24
Q

What do butchers use to make the meat look fresh?

A

Ascorbic acid to reduce methemoglobin. There is an enzyme methemoglobin reductase that converts methemoglobin to regular haemoglobin

25
Q

What percentage of haemoglobin is methemoglobin ?

A

1-2%

26
Q

What happens if there is more 10% of methemoglobin?

A

It causes symptoms (headache to seizures)

27
Q

What happens if there is more than 70% ?

A

Death

28
Q

Increased Methemoglobin can be caused by ?

A

Drugs (eg. Benzocaine) and environmental agents (nitrites, arsine etc)

29
Q

Hb subunits independently compete for O2 for ?

A

The first oxygen molecule to bind

30
Q

When the YO2 is close to 1 i.e. 3 subunits are occupied by O2 ?

A

O2 binding to the last site is independent of the other sites

31
Q

However by extrapolating slopes: the 4th O2 binds to haemoglobin 100 fold greater affinity than ?

A

The first Oxygen

32
Q

When one molecule binds, what happens ? and when one is released, what happens ?

A

When one molecule binds, the rest bind and when one is released, the rest are released

33
Q

D-2,3-Bisphosphoglycerate (BPG) binds to ?

A

Haemoglobin

34
Q

What is meant by “stripped” haemoglobin ?

A

It means BPG has been removed from the solution. This is done by adding concentrated NaCl

35
Q

Explain a right shift (easy oxygen delivery) in Hb-oxygen dissociation curve ?

A
  • High BPG
  • High H+
  • High CO2
  • HbS
36
Q

Explain a left shift (give up oxygen less readily) in Hb-oxygen dissociation curve ?

A
  • Low BPG

- HbF

Biological Chemistry (15 decks)

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