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Molecular Biology Lab. > Lab 7. > Flashcards

Lab 7. Flashcards

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1
Q

What kind of proteins is haemoglobin?

A

A heme protein.

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2
Q

What is the prosthetic group found within haemoglobin?

A

A heme group.

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3
Q

What will the heme group of haemoglobin reversibly bind to?

A

Oxygen.

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4
Q

What kind of cells is haemoglobin found in?

A

Exclusively in red blood cells (RBCs).

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5
Q

What is the job of haemoglobin in RBC’s?

A

It transports oxygen from the lungs to the rest of the body.

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6
Q

What structure does haemoglobin take up?

A

A tetramer. is made up of four subunits or two identical dimers (αβ)1 and (αβ)2 . Each subunit is composed of a polypeptide chain.

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7
Q

How is the haemoglobin tetramer made up?

A

It is made up of four subunits or two identical dimers.

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8
Q

What are the 4 subunits of haemoglobin?

A

2 alpha subunits.

2 beta subunits.

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9
Q

What is each haemoglobin subunit composed of?

A

A polypeptide chain.

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10
Q

What are the 2 conformations of haemoglobin?

A

The T conformation.

The R conformation.

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11
Q

What is the T conformation of haemoglobin?

A

The form of haemoglobin that is not bound to oxygen.

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12
Q

What is the R conformation of haemoglobin?

A

The form of haemoglobin that is bound to oxygen.

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13
Q

What kind of bonds are found between the hb subunits whilst they are in the deoxygneated state?

A

Weak ionic and hydrogen bonds.

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14
Q

What kind of bonds are found between the hb subunits whilst they are in the oxygneated state?

A

Some of the hydrogen bonds are broken so that it can weakly bind to oxygen.

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15
Q

Where is the α-globin gene located in the genome?

A

On the short arm of chromosome 16.

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16
Q

Where is the β-globin gene located in the genome?

A

On the short arm of chromosome 11.

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17
Q

How many copies of the α-globin gene are located on chromosome 16?

A

2.

α-1 and α-2.

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18
Q

How are the α and β-globin genes arranged on their respective chromosomes?

A

As 3 exons and 2 introns.

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19
Q

What are haemoglobinopathies?

A

A group of genetic disorders.

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20
Q

What causes haemoglobinopathies?

A

The production of an abnormal hemoglobin molecule.

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21
Q

What are 4 examples of haemoglobinopathies?

A

Sickle cell anaemia (Hb S).

Haemoglobin C disease (Hb C).

Haemoglobin SC disease (Hb SC).

Thalassemia.

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22
Q

What is thalassemia?

A

When a person synthesises low quantities of normal hemoglobin.

23
Q

What variant of haemoglobin do people with sickle cell have?

A

A variant called haemoglobin S or sickle haemoglobin.

24
Q

How many alleles for sickle cell must a person inherit in order for them to exhibit the trait?

A

2.

25
Q

What is the variant form of adult haemoglobin that leads to sickle cell?

A

Hemoglobin S (Hb S).

26
Q

What is the normal form of adult haemoglobin?

A

Haemoglobin A (Hb A).

27
Q

What kind of mutation leads to sickle cell disease?

A

A single nucleotide substitution (a point mutation).

28
Q

How does the SNP that leads to sickle cell change the amino acid sequence?

A

It replaces a glutamic acid with a valine.

29
Q

How does the SNP that cuases sickle cell change the triplet code?

A

It changes CAG to CTG.

30
Q

How does sickle cell affect the binding properties of haemoglobin?

A

It affects the binding ability of haemoglobin to oxygen.

31
Q

What kind of genetic disorder is sickle cell disease?

A

An autosomal Recessive Disorder.

32
Q

How do the individual properties of glutamic acid affect the side chains that they create?

A

Glutamic acid creates a polar side chain.

Valine creates a nonpolar hydrophobic side chain.

33
Q

How do the nonpolar/hydrophobic properties of valine affect the shape of the deoxygenated form of haemoglobin?

A

It causes the polymers to stiffen and distort the RBC into a sickle shape.

34
Q

How does the distortion of polymers within a red blood cell affect the lifespan of red blood cells?

A

Sickle-shaped RBCs die prematurely and this leads to a shortage of RBCs.

35
Q

What condition is caused by a shortage of red blood cells?

A

Anaemia.

36
Q

How does the sickle shape of red blood cells affect small blood vessels?

A

Sickle shaped RBCs can block small blood vessels, this can lead to the death of nearby cells or organ damage.

37
Q

What are 8 common symptoms of sickle cell anaemia?

A

Tiredness.

Anemia.

Growth retardation.

Infection.

Chronic pain in any body part

Ulcers.

Renal dysfunction.

Stroke.

38
Q

What is the worlds largest genetic disorder?

A

Sickle cell disease.

39
Q

What kind of people are mainly affected by sickle cell disorder?

A

People of African, Caribbean,Middle Eastern, Eastern Mediterranean and Asian origin.

40
Q

Who discovered sickle cell disease in 1910?

A

Dr. Herrick.

41
Q

What are 5 methods of managing sickle cell disease?

A

Prevent the deoxygenation of tissues.

Keep hydrated.

Avoid infection.

Balanced diet.

Regular medical check ups.

42
Q

What are 4 common treatments of sickle cell disease?

A

Medication.

Transfusion.

Bone marrow transplantation.

Gene therapy.

43
Q

Why is the mobility of Hb S altered during agarose gel electrophoresis at an alkaline pH?

A

Becuase the HB-S is missing the negatively charged glutamate in the β-globin chain.

This makes Hb S less negative than Hb A.

44
Q

What are 3 methods of detecting sickle cell anaemia via targeted mutation analysis?

A

ASO.

RFLP.

PCR.

45
Q

What are the 2 restriction endonucleases that are used to detect sickle cell via RFLP?

A

DdeI or Mst-II.

46
Q

What method can be used to detect sickle cell via prenatal diagnosis?

A

FISH.

47
Q

What 2 methods can be used to detect sickle cell via preimplantation genetic analysis?

A

PCR.

FISH.

48
Q

Can DNA sequencing be used to detect sickle cell?

A

Yes.

49
Q

What is the basis of the RFLP test for sickle cell disease?

A

That restriction enzymes will recognise specific restriction sites within a DNA sequence.

50
Q

What are the normal 3 codons that specify amino acids 5, 6 and 7 in the β-globin gene?

A

CCT- GAG-GAG.

Pro-Glu-Glu.

51
Q

What are the abnormal 3 codons that specify amino acids 5, 6 and 7 in the β-globin gene?

A

CCT-GTG-GAG.

Pro-Val-Glu.

52
Q

What is the recognition site for the MST-II enzyme?

A

CCTNAGG.

53
Q

How does the mutated form of the β-globin gene affect the cleavage site for MST-II?

A

Mst-II cannot recognise the T that replaces the A in the new sequence.

Molecular Biology Lab. (7 decks)

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