Proteins Flashcards

1
Q

What is the primary sequence of a protein forming?

A

The order of amino acids in a polypeptide chain are formed and stabilised by peptide bonds

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

What is the secondary structure of a protein forming?

A

The polypeptide chain may form into α-helixes or β-pleared sheets and are stabilised by hydrogen bonds

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

What is the tertiary structure of a protein?

A

the polypeptides fold into three-dimensional structures which determine their function and are stabilised by hydrogen bonds, disulfide bridges and hydrophobic reactions. Some proteins do not develop further

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

How do polypeptides behave in an acqeous environment during the tertiary stage

A

the polar side chain form hydrogen bonds to water while the nonpolar side chains are packed into a hydrophobic ‘core region’

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

What is the quaternary stage of a protein?

A

two or more polypeptides may assemble to form larger proteins

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

What is a protein?

A

A sequence of amino acids wherein each amino acid has a carboxyl and amino functional group attached to a carbon atom

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

How are amino acids distinguished from each another?

A

Their side group (r-group)

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

What happens if proteins are misfolded?

A

The function of said protein may change or the protein might lose its function

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

Why might a proteins structure change?

A

Due to interactions with other molecules or enzymatic processes

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

What determines protein activity?

A

The polypeptides ability to bind to other proteins or molecules

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

What is the main function of enzymes?

A

To catalyse biochemical reactions

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

How do enzymes catalyse reactions?

A

By lowering the activation energy required for a reaction to proceed

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

What are three (non-negative regulation) factors which affect how proteins function?

A

Subcellular localisation, association with other proteins and ligand binding

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

What is negative regulation of a protein?

A

Mechanisms which inhibit proteins function

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

What are three forms of negative regulation?

A

Allosteric inhibition, inhibitory proteins, feedback inhibition

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

Describe allosteric inhibition

A

A process where certain molecules bind to an enzyme in a location other than the active binding site, reducing the enzymes activity

17
Q

What are inhibitory proteins?

A

Proteins which can bind to target proteins to inhibit their functuins

18
Q

What is feedback inhibition?

A

A process within metabolic pathways where the product of a chain of reactions acts as an inhibitor in an earlier step, in order to maintain metabolic balance