Protiens (Structure, Folding And Function)

Question 1

What enzyme forms peptide bonds

Answer 1

Peptidyl transferase

Question 2

Describe peptide bonds

type of bond, between what constituents

Answer 2

Covalent bonds

Formed between the carboxyl group (COOH) of one amino acid residue and the amino group (NH2) of another

Question 3

What constituent of an amino acid determines a protein’s classification

Answer 3

It’s R group

Question 4

What is found at the N terminal of proteins

Answer 4

Amino (NH3+) group

Question 5

What is found at the C terminal of a protein p

Answer 5

Carboxyl (COO-) group

Question 6

Describe a protein’s ‘Primary Structure’

Answer 6

The sequence of amino acids that make the protein

Question 7

Describe what is meant by a protein’s ‘secondary structure’

AND give 2 examples

Answer 7

The arrangement of the polypeptide backbone into a repeating pattern

AND

(Alpha Helix and B pleated sheet)

Question 8

Describe what is meant by ‘Tertiary Structure’

Answer 8

Side chain interactions that causes the overall 3D configuration of the protein

Question 9

Describe ‘Quaternary Structure’

Answer 9

Association between different polypeptides chains

Question 10

What is the BYPRODUCT when 2 amino acids are linked

Answer 10

Water 💧

Question 11

What are 4 properties of peptide bonds

Answer 11

1 - Planar
2 - Rigid
3 - Bonds on either side of the peptide bond can rotate freely
4 - They exhibit a trans confirmation

Question 12

Why are peptide bonds rigid

Answer 12

They exhibit partial double bond characteristics

Question 13

What is a benefit of proteins exhibiting a trans confirmation

Answer 13

It avoids steric clashes

Question 14

Define the ‘Isoelectric Point’ of proteins

Answer 14

The pH at which there is no overall net charge