Topic 3 (proteins recap)

Question 1

What is the proteome

Answer 1

Full set of proteins encoded by human genome

Question 2

What is disrupted in phyenylketonuria?

Answer 2

Phenylalanine hydroxylase

Question 3

What happens in phyenylketonuria

Answer 3

No breakdown of AA pheynlalanine

Permanent brain damage

Question 4

What is missing in haemophilia

Answer 4

Factor 8

Question 5

Duchenne muscular dystropy is caused by what?

Answer 5

Dystrophin muscle protein absent/ineffective

Question 6

Collagen mutation can lead to what?

Answer 6

Osteogenesis imperfecta

Question 7

What causes scurvy

Answer 7

Lack of vit c leads to lack of collagen production

Question 8

Why is vit.c associated with scurvy?

Answer 8

Vitamin C is cofactor for hydroxylases during collagen synthesis

Question 9

Myasthenia gravis is caused by what?

Answer 9

Antibody to neurotransmitter receptor

Question 10

Name the 9 non polar AA

Answer 10

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

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Question 11

Name the 6 polar AA

Answer 11

Serine, Threonine, Cysteine, Asparagine, Glutamine, Tyrosine

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Question 12

Name the 2 acidic AA

Answer 12

Aspartic Acid, Glutamic Acid

Question 13

Name the 3 basic AA

Answer 13

Lysine, Arginine, Histidine

Question 14

All amino acids are what except glycine?

Why?

Answer 14

all AA are chiral

Glycine only has Hydro as R group

Question 15

Which isomer is found in proteins?

Answer 15

L amino acids

Question 16

pka of Carboxylic groups

Answer 16

1.8-2.5

Question 17

pka of A-amino groups

Answer 17

9-10

Question 18

pka of histidine

Answer 18

6

Question 19

definition of pka

Answer 19

pH where 50% of group is ionised

Question 20

typical proteins have how many AA

Answer 20

50-2000

Question 21

What reaction forms a peptide bond?

Answer 21

Condensation reaction

Question 22

Why is trans peptide bond common

Answer 22

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

Question 23

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

Answer 23

N-H

C=O

4 residues

Question 24

Does alpha contain interchain bonds?

Answer 24

no only B sheets have intrachain and interchain

Question 25

R group is found on what part of a B sheet

Answer 25

Outside plane of sheet

Question 26

What type of amino acids are Hydrophobic? Where are they found in a protein

Answer 26

Non-Polar Interior of soluble protein

Question 27

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

Answer 27

Disulphide covalent Non covalent (Van der Waals/Hbonds)

Question 28

What type of reaciton forms disulphide bonds

Answer 28

Oxidation reaction between pair of cysteine = cystine

Question 29

How are salt bridges formed?

Answer 29

Oppositely charged side chains

Question 30

How do Dipoles form?

Answer 30

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

Question 31

With dipoles and Van Der Waals, what occurs?

Answer 31

temporary / induced dipoles are being constantly produced

Question 32

What type of AA can H-bond

Answer 32

Polar residues

Question 33

What do chaperones do?

Answer 33

Bind to short segments of protein Facilitates correct folding

Question 34

What do chaperonins do?

Answer 34

Form folding chambers Providing stable environment for correct folding Prevents aggregation

Question 35

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

Answer 35

cerebral cortex

Question 36

What aggregates in Alzheimers?

Answer 36

Insoluble fibres of Amyloid B protein = plaque

Question 37

Creutzfeldt jacob disease leads to what 3 things

Answer 37

memory loss loss of co-ordination coma

Question 38

What causes CJD

Answer 38

Prion Protein PrP^sc

Question 39

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

Answer 39

Insoluble aggregates form

Question 40

BSE is caused by what?

Answer 40

Infectious protein agent