proteins 1 Flashcards

1
Q

what is an amino acid made up of?

A

central carbon attached to a H, R, Carboxylic acid group and an amino group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

what is a codon

A

a triple base sequence which codes for an amino acid. the aminoacid is determined by the first base

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

what types of amino acid are there and what do they mean?

A

1- aliphatic-only C and H
2-aromation-contains a cyclic aromatic ring
3-basic- tend to have a positive charge due to an extra NH2
4- acidic-tend to have a negative charge due to an extra COO-

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what its a peptide bond?

A

a covalent bond which forms between two adjacent amino acids to form a polypeptide and one molecule of H2O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

where does the peptide bond form?

A

in ribosome during translation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

define primary structure

A

the sequence of amino acids in a polypeptide chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

define secondary structure

A

the spatial arrangement of amino acid residues which are near each other in a linear sequence.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

describe the two types of secondary structure

A

Alpha-helix: telephone wire shape. H-bonds between the H-N and the C=O every 4 amino acid residues.
Beta-pleated sheets: H-bonds between amide groups of linear polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

define tertiary structure

A

the spatial arrangement of aminoacid residues which are far away from each other in the polypeptide chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

hydrogen bonds

A

1/20th the strength of a peptide bond
stronger than VDWs
forms with F,O,N

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

VDWs

A

weak interactions within the tertiary structure.

there are many of them. every 0.3 nm

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

disulphide bridges

A

between cysteine containing groups

Found in lots of extracellular proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

ionic bonds

A

between amino acid residues with oppositely charged R groups.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

quartenary structure

A

the spatial arrangement of individual polypeptide chains in a multi-subunit protein.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

denaturation

A

when the secondary and tertiary structure bonds are broken. it alters the shape and , hence the function of the protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

causes of denaturation?( 6)

A
1-heat
2-solvents
3-acids
4-cross-linking reagents e.g. formaldehyde
5-disulphide-bond reducers
6-chaotrpic agents e.g. urea
17
Q

how to break the primary structure?

A

to break the primary structure the peptide bonds must be broken.
peptidases are used.
EXO peptidases- break off a single amino acid at one time.
ENDO peptidases- break off the aminoacid from the middle
CARBOXY peptidases- break off the peptide bond from the coo
AMINO peptidases- break off the peptide bond from the NH2

18
Q

what does denaturation cause?

A

1- decreases solubility
2-alters water-binding abilities
3-loss of biological activity
4-improves digestibility