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IMS > Topic 3 (proteins recap) > Flashcards

Topic 3 (proteins recap) Flashcards

1
Q

What is the proteome

A

Full set of proteins encoded by human genome

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2
Q

What is disrupted in phyenylketonuria?

A

Phenylalanine hydroxylase

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3
Q

What happens in phyenylketonuria

A

No breakdown of AA pheynlalanine

Permanent brain damage

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4
Q

What is missing in haemophilia

A

Factor 8

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5
Q

Duchenne muscular dystropy is caused by what?

A

Dystrophin muscle protein absent/ineffective

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6
Q

Collagen mutation can lead to what?

A

Osteogenesis imperfecta

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7
Q

What causes scurvy

A

Lack of vit c leads to lack of collagen production

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8
Q

Why is vit.c associated with scurvy?

A

Vitamin C is cofactor for hydroxylases during collagen synthesis

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9
Q

Myasthenia gravis is caused by what?

A

Antibody to neurotransmitter receptor

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10
Q

Name the 9 non polar AA

A

Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Phenylalanine, Tryptophan, proline

GAVLIMFWP
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11
Q

Name the 6 polar AA

A

Serine, Threonine, Cysteine, Asparagine, Glutamine, Tyrosine

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12
Q

Name the 2 acidic AA

A

Aspartic Acid, Glutamic Acid

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13
Q

Name the 3 basic AA

A

Lysine, Arginine, Histidine

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14
Q

All amino acids are what except glycine?

Why?

A

all AA are chiral

Glycine only has Hydro as R group

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15
Q

Which isomer is found in proteins?

A

L amino acids

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16
Q

pka of Carboxylic groups

A

1.8-2.5

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17
Q

pka of A-amino groups

A

9-10

18
Q

pka of histidine

A

6

19
Q

definition of pka

A

pH where 50% of group is ionised

20
Q

typical proteins have how many AA

A

50-2000

21
Q

What reaction forms a peptide bond?

A

Condensation reaction

22
Q

Why is trans peptide bond common

A

Most advantageous due to Oxy and Hydr on opposite side of bond

23
Q

H bonds occur between that two types of bonds ion A helix every …. residues

A

N-H

C=O

4 residues

24
Q

Does alpha contain interchain bonds?

A

no only B sheets have intrachain and interchain

25
Q

R group is found on what part of a B sheet

A

Outside plane of sheet

26
Q

What type of amino acids are Hydrophobic?

Where are they found in a protein

A

Non-Polar

Interior of soluble protein

27
Q

What type of bonds are present in Quaternary / tertiary bonding to stabilise structures

A

Disulphide covalent

Non covalent (Van der Waals/Hbonds)

28
Q

What type of reaciton forms disulphide bonds

A

Oxidation reaction

between pair of cysteine = cystine

29
Q

How are salt bridges formed?

A

Oppositely charged side chains

30
Q

How do Dipoles form?

A

2 atoms of opposing charge share electrons, however electrons tend to lean to one atom more than another leading to unequal sharing

31
Q

With dipoles and Van Der Waals, what occurs?

A

temporary / induced dipoles are being constantly produced

32
Q

What type of AA can H-bond

A

Polar residues

33
Q

What do chaperones do?

A

Bind to short segments of protein

Facilitates correct folding

34
Q

What do chaperonins do?

A

Form folding chambers

Providing stable environment for correct folding

Prevents aggregation

35
Q

Loss of neurons in what part of the brain occur in alzheimer’s

A

cerebral cortex

36
Q

What aggregates in Alzheimers?

A

Insoluble fibres of Amyloid B protein = plaque

37
Q

Creutzfeldt jacob disease leads to what 3 things

A

memory loss

loss of co-ordination

coma

38
Q

What causes CJD

A

Prion Protein

PrP^sc

39
Q

If abnormal PrP^sc forms with a helical PrP^sc, what occurs

A

Insoluble aggregates form

40
Q

BSE is caused by what?

A

Infectious protein agent

IMS (25 decks)

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