Protein stability and folding

Question 1

What confers protein stability?

Answer 1

The interactions between the protein’s atoms and the atoms in the solvent it finds itself in.

Question 2

Examples of non-covalent bonds

Answer 2

1. electrostatic forces
2. hydrophobic forces

Question 3

Examples of electrostatic forces

Answer 3

1. hydrogen bonds
2. ionic bonds
3. Van der Waals forces

Question 4

Describe non-covalent bonds

Answer 4

These are low energy, interactions that allow for the maintenance of 3D structures of proteins by providing specific and transient bonding of large molecules.

Question 5

Example of covalent bonds

Answer 5

Disulphide bonds

Question 6

True or false. The amino group is a hydrogen donor.

Answer 6

True

Question 7

True or false. The carboxyl group is hydrogen acceptor

Answer 7

True

Question 8

What are van der Waals forces

Answer 8

associations between electronically neutral molecules

Question 9

What is the major force driving protein folding

Answer 9

Hydrophobic forces

Question 10

What functions are disulphide bonds included in?

Answer 10

They have catalytic function where by redox catalyst makes or breaks disulphide bonds regulate the activity of proteins. They can switch enzymes off, cause confirmation changes and alter binding ability.