Amino Acids Flashcards

1
Q

This is responsible for the properties of amino acids and is often the differentiating factor.

A

Side chains

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

How many amino acids are there?

A

20

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

What are the 4 categories of amino acids?

A

Polar, non-polar, and charged (at physiological pH)

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

What are the 2 ways in which one letter abbreviations can be helpful?

A

To identify mutations and sequence alignment

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

This is the pH at which the group is 50% ionised.

A

pKa

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

This is the pH at which net charge on an amino acid/protein is zero

A

pI/isoelectric point

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

How are ionisable side chains classified?

A

Through their pKa

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

This is the addition of a chemical group to an amino acid residue after translation has occurred.

A

Post translational modification

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

What does PTM do?

A

Modifies the function of a protein; like, in a way that will switch it on/off, direct cellular location, targets for degradation

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

This is the bond formed between cysteine molecules.

A

Disulfide bond

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

This is often used to control enzyme activity (turn it on/off using chemical). Often characterised by having a phosphate group added to an enzyme.

A

Phosphorylation

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

This is an amino acid modification used to prevent connective tissues and scurvy.

A

Hydroxylation

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

This type of amino acid modification often involves proline and lysine.

A

Hydroxylation

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

This is needed for blood clotting, often involves glutamate

A

Carboxylation

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

This is the process of adding sugar groups to biomolecules.

A

Glycosylation

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

What are the 3 main properties of peptide bonds?

A

They are planar/flat, trans (a-carbons go on opposite sides), has a dipole

17
Q

How are peptide bonds formed?

A

Dehydration reaction between C-terminal (of one amino acid) and N-terminal of another amino acid

18
Q

This is a short stretch of amino acids joined together by peptide bonds.

A

Peptide

19
Q

This is a longer chain of amino acids joined together with a defined biological function.

A

Protein

20
Q

This is formed when amino acids are covalently bonded together in a peptide or a protein.

A

Amino acid residues

21
Q

Where are the side chains attached?

A

Protein main chain

22
Q

What are proteins polymers of?

A

Amino acids

23
Q

What are the main techniques used to determine protein structure?

A

crystallography, spectroscopy and cryo electron microscope