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IMS > Topic 3 (Proteins Health) > Flashcards

Topic 3 (Proteins Health) Flashcards

1
Q

What type of proteins contain keratin/collagen

A

Fibrous proteins

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2
Q

What type of proteins have repeated AA sequences and have a high hydrophobic AA content

A

Fibrous proteins

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3
Q

What type of proteins are soluble

A

Globular

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4
Q

What % of abnormal haemoglobins is caused by a single AA change?

A

95%

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5
Q

Whats the role of myoglobion?

A

Stores O2 in tissue

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6
Q

Where is myoglobin found predominantly

A

skeletal / cardiac muscle

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7
Q

Structure of myoglobin (helices)

A

8 a-helices

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8
Q

What group does myoglobin contain?

What does this comprise of (2)

A

Haem prosthetic group

Fe(2+) + Protoporphyrin IX

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9
Q

What is haem comprise of? What bonds are present?

A

9 ring

Covalent bonds

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10
Q

What does Proximal Histidine bind to?

What number/symbol is it denoted?

A

Binds to Iron

F8

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11
Q

What does Distal Histidine bind to?

What number/symbol is it denoted?

A

Binds to O2

E7

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12
Q

When Oxygen binds to haem, what moves?

A

Iron moves closer to E7

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13
Q

Structure of Haemoglobin (a/b)

How is it all held together by?

How many O2 can it carry

A

2a / 2b

non covalent bonds

4O2

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14
Q

By how much does haemoglobin differ to myoglobin

A

Differs by 83% AA

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15
Q

What type of protein is haemoglobin in regards to the fact it changes shape

A

Allosteric

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16
Q

Which protein has a higher affinity for oxygen

A

Myoglobin

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17
Q

When haemoglobin binds to Oxygen, conformational changes occur which ruptures what?

What does this allow?

A

Salt bridges rupture

Increases affinity for O2

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18
Q

Which state of haemoglobin is tense and has low affinity for oxygen

What type of bonds are present

A

T state

Many salt bridges

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19
Q

The Bohr effect is based off what principle?

A

Decreasing pH = Decreases affinity for O2

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20
Q

When H+ are high, what AA is protonated?

What does this prevent

A

Histidine residues are protonated

Removes affinity for O2

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21
Q

When H+ is high, what type of AA are protonated?

What does this cause?

A

+ charged AA

Forms salt bridges = T state = decreases affinity for O2

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22
Q

BPG stands for what?

Where is it found in high concentrations

A

Biphosphoglycerate

Erythrocytes

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23
Q

How is BPG increased?

A

hypoxia / high altitudes

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24
Q

What does BPG do to haemoglobin?

A

Decreaes affinity for O2

25
Q

How does BPG work?

A

Binds only in T state to B subunits

-charge on BPG reacts with +AA residues

26
Q

Foetal HB structure

A

a2y2 (HbF)

27
Q

Out of haemoglobin / myoglobin / Foetal Hb, which has the strongest affinity to O2

A

HbF

28
Q

Give 2 examples of haemoglobinopathies

A

Sickle cell

B thalassaemia

29
Q

What are the two positions that are a critical AA involved with haem functioning correctly (haem contact)

A

Phe // Leu (hydrophobic)

CD1 / F4

30
Q

What type of substitution still allows funcitoning haemoglobin?

A

Conservative substitution

31
Q

If Alanine is substituted for isoleucine, what occurs in haemoglobin?

A

Nothing… both are hydrophobic

32
Q

If Leucine is substituted by Lysine, what occurs in haemoglobin?

A

Major effect on structure / function

33
Q

Which type of collagen are most common?

A

types 1/2/3

34
Q

Which type of collagen are found in the basal lamina?

A

Types 4/7

35
Q

which type of collagen are fibril associated collagens?

A

Types 5,9, 12

36
Q

Polypeptide synthesis of collagen occurs in which cell?

A

Fibroblasts

37
Q

What sort of structure is formed before being secreted out of cell?

A

Procollagen triple helical cable

38
Q

Which type of collagen has extension proteins?

A

Procollagen

39
Q

What is cleaved off in procollagen? Where is this done?

A

Extension peptides

Extracellular spaces of CT

40
Q

What forms microfibrils?

A

Tropocollagen

41
Q

Which AA is repeated every 3rd residue?

A

Glycine

42
Q

What modified AA are present in collagen?

What process is done to modify these AA?

A

Hydroxyproline // Hydroxylysine

Hydroxylation

43
Q

When does Hydroxylation occur?

A

Before Polypeptide chain forms a helix

44
Q

Role of Hydroxyproline?

A

Stabilises triple helix via H bond formation

45
Q

Role of Hydroxylysine?

A

Attachment sites for sugar residues

46
Q

What handed helix is each individual chain in collagen?

What is the overall direction of tropocollagen?

A

Left handed helix

Forms right handed twist

47
Q

Glycine is found where in the helix?

A

Packed into centre of chain

48
Q

Where do disulphide bonds form in assembly of collagen?

A

Between C terminal extensions

49
Q

What is role of lysyl oxidase / allysine oxidase in collagen production?

A

Stabilising fibrils from tropocollagen via covalent cross links

50
Q

Holes between tropocollagen fibres form what?

A

Nucleation sites for Ca deposition

51
Q

Role of collagenases?

A

Repair breakdown of collagen

52
Q

What are collagenases?

A

Metalloproteinases

53
Q

Where are collageneases found in high volume?

A

Tumour cells for invasion / metastasis

54
Q

What contracture produces excess collagen in hand

A

Dupuytrens contracture

55
Q

What treatment can be given for Dupuytrens contracture

A

Injection of collagenases

56
Q

Ehlers Danlos syndrome is caused by what?

A

Lysyl oxidase deficiency

57
Q

Symptoms of Ehlers Danlos Syndrome (4)

A

Joint hypermobility
extreme fatigue
stretchy skin
digestive problems

58
Q

Osteogenesis is caused by what?

A

Spontaneous mutation in type 1 collagen

59
Q

which type of osteogenesis is the worst for prognosis

A

Type 4

IMS (25 decks)

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