Proteins Flashcards

Unit 2: Biomolecules

1
Q

What do proteins contain?

A

Carbon, Hydrogen, Oxygen, NItrogen and sometimes Sulphur

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

What are proteins composed of?

A

They are cmoposed of long chains of monomers called amino acids

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

What do each amino acids contain?

A

They contain a central alpha carbon linked to an amine group, carboxyl group, and variable (R) group and a hydrogen atom.

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

What do amino acids differ by?

A

Amino acids differ in the composition of their variable side chain (R)

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

How are dipeptide formed?

A

Two amino acids joined by condensation

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

How are polypeptide formed?

A

They are formed by more amino acids being added to the dipeptide

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

What catalyzes the condensation reactions?

A

Ribosomes

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

What is a peptide bond?

A

Bond linking amino acids together (C-N bond, -NH2 of one amino acid and -COOH of the other)

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

Define essential amino acid

A

Acids that animals cannot synthesize (make) and must be obtained from diet

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

Define non-essential amino acids

A

Acids that can be made by animals using pathways that transform one amino acids into another

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

What can shortage of one or more essential amino acids in diet cause?

A

They can prevent the production of specific proteins

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

Ribosome’s function in amino acids?

A

Ribosomes can join amino acids between any pair of the 20 different amino acids

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

Functions of R groups?

A

R groups stabilize the 3D shape of proteins

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

Define denaturation

A

When there is a conformational change in a protein, they don’t normally return to their original structure, it’s usually permanent

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

What can cause denaturation?

A

Heat, due to vibrations in the molecule
Extreme pH

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

What do R groups determine?

A

They determine the vehicle properties of amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Define Conformation

A

3D shape

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What decides which level the proteins conforms to

A

It’s decided by it’s amino acid structure

19
Q

What do each proteins conforms into determine

A

It deterines the fuction of the protein?

20
Q

What are four levels of protein structure?

A

Primary Structure
Secondary Structure
Tertiary Structure
Quaternary Structure

21
Q

Primary Structure

A

Sequence of amino acids
Formed by peptide bonds
Determines/controls the other levels

22
Q

Secondary Structure

A

Folds/turns of amino acid sequence upon themselves
Pattern of H bonds between amine and carboxylic groups creates the secondary structure
H bonds give stability
Fibrous proteins

23
Q

Tertiary Structure

A

3D folding pattern due to side chain interactions
Polypeptide folds and coils (complex)
Caused by interactions between R groups
Tertiary shape is very important for function
Globular proteins

24
Q

Quaternary Structure

A

Interaction between multiple polypetides
Sometimes prosthetic (part that is not an amino acid) groups involved
Classified as fibrous or globular

25
Define Alpha helix
The structure when the chain coils
26
Define beta-pleated sheet
The structure when teh chain pleats
27
Is C=O polar or non-polar
Polar
28
Is N-H polar or non-polar
Polar
29
Where are H bonds formed
H bonds are formed readily along a polypeptide chain
30
Functions of H bonds in polypeptide chain
Although individually H bonds are weak, there are so many that it helps to stabilize
31
Types of bonds in tertiary structure
Ionic bonds - between + and - R groups Hydrogen bonds - between polar R groups Disulfide bridges Hydrophobic interactions
32
What can amino aicds in proteins broadley be catagorized as?
They can be catagorized as being either hydrophobic (non-polar) or hydrophilic (polar/charged)
33
Example of polar and non-polar amino acids on tertiary structure of globular proteins
Globular proteins need to be soluble in water so the outside/surface amino acids are hydrophilic where they contact water and center is hydrophobic
34
What do the arrangement of polar and non polar amino acids affect?
Tertiary structure, they help them stabilize and ensure position is maintained that suits the proteins function
35
Define non-conjugated proteins
They have only polypeptide subunits
36
Example of non-conjugated proteins
Insulin is 2 polypeptides joined by a disulphide bridge
37
Define conjugated proteins
Have one or more non-polypeptide chains called prosthetic groups, in addition to teh polypeptides
38
Example of conjugated proteins
Haemoglobin - 4 polypeptide chains and each with a haem group. Increasing the diversity of the protein, allowing more function
39
Define fibrous proteins
Contain elongated polypeptides that lack folding or alpha helices
40
Example of fibrous proteins
Collagen, rope like structure giving high tensile strength
41
Define Globular proteins
Rounded shape due to folding, intricate shape stabilized by R group bonds, exact shape closely related to its function
42
Example of globular proteins
Enzymes, receptor sites. Only insulin hast he right shape to connect to the insulin receptor
43
What does the connection between insulin and insulin receptor cause
They cause signals to be sent that open channels to move glucose into cells