2.4 Proteins Flashcards

1
Q

What is the monomer that forms proteins?

A

Amino Acids

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

What is the structure of an amino acid?

A

Central carbon bound to:

  • An amine group (NH2)
  • A carboxyl group (COOH)
  • A hydrogen atom
  • A variable side chain (R)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

How many amino acids exist universally?

A

20

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

What do we call a chain of amino acids?

A

Polypeptide

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

Are polypeptides polar?

A

They differ in structure, some are some are not

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

What type of bond holds amino acids together?

A

(Covalent bonds) called peptide bonds

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

How are polypeptides broken down?

A

Hydrolysis

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

Between which groups do peptide bonds form?

A

Carboxyl and Amine group

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

What is the primary structure of amino acid sequences?

A

The order

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

What is the secondary structure of amino acid sequences?

A

How the amino acids are folded

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

What is the tertiary structure of amino acid sequences?

A

The overall 3D configuration

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

What is the quaternary structure of amino acid sequences?

A

The structure including any other polypeptide strands which may or not be present

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

What are the two stable configurations of amino acid secondary structures?

A

Alpha helices

Beta-pleated sheets

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

Describe alpha helix structure

A

Amino acids fold in a coil/ spiral arrangement

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

Describe beta-pleated sheets

A

Directionally-oriented staggered strand conformation

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

How do alpha helices and beta pleated sheets form?

A

Hydrogen bonds form between non-adjacent amine and carboxyl groups

17
Q

What determines the tertiary strucutre?

A

Interactions between the variable chains

18
Q

Give an example of a protein with a quaternary structure

A

Haemoglobin

4 polypeptide chains and an iron-containing haeme group

19
Q

What is a prosthetic group?

A

A non amino-acid component that is part of a protein

20
Q

Define denaturation

A

Is a structural change in a protein that results in the loss (usually permanently) of its biological properties

21
Q

Which two factors can cause denaturation?

A

pH

temperature

22
Q

How does temperature cause denaturation?

A

High levels of thermal energy can break the hydrogen bonds

23
Q

How does pH cause denaturation?

A

The pH can alter the charge of the protein, altering it’s solubility and shape

24
Q

What is the process of converting a gene sequence into a polypeptide?

A

Transcription

Translation

25
Q

How many polypeptides do genes typically code for?

A

Usually 1 but there are exceptions

26
Q

When do genes code for more than one polypeptide?

A
  • Genes may be alternatively spliced to generate multiple polypeptide variants
  • Genes encoding tRNA sequences are transcribed but never translated
  • Genes may be mutated and consequently produce an alternative polypeptide sequence
27
Q

What is the proteome?

A

The totality of proteins expressed within a cell, tissue or organism at a certain time

28
Q

Why may a proteome be significantly larger than the number of genes?

A
  • Alternative splicing (creating more than one protein from a single gene)
  • Modification after translation to promote further variants
29
Q

What purposes may a protein serve?

A
Structure
Hormones
Immunity
Transport
Sensation
Movement
Enzymes