Proteins Flashcards

(62 cards)

1
Q
Which of the following groups on an amino acid determines its chemical properties:
hydrogen
a-amino
a-carboxyl
R group
A

R group

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2
Q
Other than:
shape
size
polarity
sulphur-containing
imino
Name another way to categorise R groups?
A

Charge

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3
Q

What are the 9 non-polar amino acids?

A
Glycine
Alanine
Valine
Leucine
Isoleucine
Methionine
Phenylalanine
Tryptophan
Proline
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4
Q

What are the polar amino acids?

A
Serine
Threonine
Cysteine
Tyrosine
Asparganine
Glutamine
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5
Q

Name the acidic amino acids.

These are negatively charged.

A

AspartATE

GlutamATE

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6
Q

Name the basic amino acids.

These are positively charged.

A

Histidine
Arginine
Lysine
(HAL)

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7
Q

Which amino acid is not optically active?

A

Glycine

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8
Q
Which type of amino acids are found in proteins:
B isomers
L isomers
D isomers
P isomers
A

L isomers

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9
Q

What stage of protein sturcture is B pleated sheets?

A

Secondary

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10
Q

What bonds join amino acids?

Where does this occur?

A

Peptide

Ribosomes

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11
Q

Do amino acids get added from C-terminus to N-terminus or N-terminus to C-terminus?

A

N –> C

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12
Q

Peptide bonds have partial double bond characteristics.

True or false?

A

True

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13
Q

What are the 2 types of secondary protein structures?

A

a-helices

B-pleated sheets

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14
Q

In a-helices where are the intrachain H bonds?

What is the function of these bonds?

A

Between N-H and C=O

Stabilise helix

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15
Q

Which residue does residue 1 join to in an alpha helix?

A

5

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16
Q

Which residue does residue 7 get joined by in an alpha helix?

A

3

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17
Q

Which residue does residue 2 join to in an alpha helix?

A

6

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18
Q

In terms of H bonding between adjacent strands in B-pleated sheets, what are:

1) Interchain H bonds
2) Intrachain H bonds

A

1) Between different amino acid chains

2) Between 2 parts of same amino acid chain

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19
Q

Where does the R group lie in relation to the B-pleated sheet?

A

Outside plane of sheet

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20
Q

What type of amino acids lie in the interior of proteins?

Give examples.

A
Hydrophobic
Leucine
Vlaine
Methionine
Phenylalanine
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21
Q

What type of amino acids lie in the exterior of proteins?

Give examples.

A
Hydrophillic
Arginine
Histidine
Lysine
Asparatate
Glutamate
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22
Q

Between which type of amino acids do salt bridges exist?

A

Oppositely charged

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23
Q

Between which amino acids do disulphide bonds exist?

A

Cysteine

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24
Q

VdW forces exist between..?

A

Neutral molecules

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25
Which precursor protein is responsible for Alzheimer's disease?
Amyloid precurson protein
26
Which protein is found in the brain that is responsible for Alzheimer's disease?
Amyloid B protein
27
What are the roles of plaques formed from the amyloid B protein fibrils in Alzheimer's disease?
Destroy neurons
28
Which protein is responsible for Creutzfeldt Jacob Disease (CJD)?
Prion protein (PrPSc)
29
Which type of proteins are elongated and insoluble?
Fibrous
30
Which type of proteins are soluble and compact?
Globular
31
What type of proteins are ion channels?
Membrane
32
Being a carrier of which two diseases provides resisatnce to malaria? How?
Thalassaemia - smaller RBCs with less haemoglobin so parasite cannot penetrate Sickle cell anaemia - RBCs sickle in response to parasite so it gets trapped
33
What is myoglobin?
An oxygen store
34
Does myoglobin have a primary, secondary, tertiary or quaternary structure?
Tertiary
35
How many alpha helices does myoglobin have?
8
36
What are the differences between haemoglobin and myoglobin in: 1) Oxygen binding 2) Oxygen affinity
1) Haem = cooperative Myo = non-cooperative 2) Haem = pH/CO2 dependent and regulated by BPG Myo = not pH/CO2 dependent nor regulated by BPG
37
What does allosteric mean?
Binding of oxygen to one subunit affects interactions with other subunits
38
What substitution takes place when oxygen binds to haemoglobin? How does this affect affinity?
His F8 --> His E7 | Increases affinity of haem subunits for oxygen
39
Does the T state or R state have a higher affinity?
R state
40
Where does BPG bind in T state?
Between beta subunits
41
At high altitudes what happens to BPG? | What is the result of this on Hb affinity for O2?
BPG increases | Reduced affinity
42
How effectively can BPG bind to foetal Hb and why?
Less effectively | Prevents reduction in affinity
43
What are the 4 invariant amino acids?
His F8 His E7 Gly B6 Pro C2
44
What is the difference between conservative and non-conservative substitution?
``` Conservative = maintains hydrophobic interior Non-conservative = has major affect on protein structure/function ```
45
Which collagen types are fibril-forming?
Types 1, 2, 3
46
Which collagen types are network-forming?
Types 4, 7
47
Which collagen types are fibril-associated?
Types 5, 9, 12
48
Which collagen type forms all basal lamina?
Type 4
49
Which collagen type forms cartilage?
Type 2
50
Which hydroamino acid is an attachment site for sugars and involved in crosslinking collagen chains?
Hydrolysine
51
Which hydroxyamino acid is responsible for stabilising the triple helix and involved in H bond formation?
Hydroxyproline
52
What is the cofactor needed for prolyl hydroxylase and lysyl hydroxylase to work?
Ascorbic acid (Vit D)
53
What disease results from excess collagen production?
Dupuytren's contracture
54
Osteogenesis imperfecta is caused by what?
Mutation in collagen chains
55
What disease results from a deficiency of lysyl oxidase?
Ehers-Danlos syndrome type VI
56
What causes scurvy?
Vit D deficiency
57
Which amino acids contain sulphur?
Cysteine | Methionine
58
Name an imino acid
Proline
59
Which amino acid is an a-helix terminator?
Proline
60
Which amino acids are aromatic?
Phenylalanine Tyrosine Tryptophan
61
What is the 21st amino acid?
Selenocysteine
62
Name a large amino acid.
Tryptophan