Lesson 5: Protein Folding

Question 1

What does the primary structure of a protein determine ?

Answer 1

It determines how a protein will fold

Question 2

Why is the primary structure formed ?

Answer 2

Due to the peptide bonding

Question 3

What are the 2 examples of chaperones ?

Answer 3

hsp70 and hsp60

Question 4

What do the 2 chaperons we learned stop ?

Answer 4

The aggregation of proteins

Question 5

What causes Alzeheimer’s ?

Answer 5

Accumalation of B-amyloid

solube aplha rich state –> insoluble B-rich state

Question 6

Which structures can renature ?

Answer 6

Secondary, Tertiary, Quaternary,

Question 7

What structure is the protein first biologically active ?

Answer 7

Tertiary

Question 8

What determines the tertiary strcutre of proteins ?

Answer 8

the interactions between the functional groups of side chains

disulfide bond, h-bond, hydrophobic interactions, salt-bridge

Question 9

What are domains ?

Answer 9

Parts of the protein that serve a specific function

Question 10

What determines the Quaternary structure ?

Answer 10

The covalent and non covalent interactions between subunit surfaces

Question 11

T/F: Hemoglobin is a dimeric protein.

Answer 11

False, Tetrameric

Question 12

What happens to the solubility and viscosity of a denatured protein ?

Answer 12

Solubility decreases and viscosity increases

Question 13

What does the quaternary structure define ?

Answer 13

The number&type of polypeptide & their spatial arrangment

Question 14

What determines the secondary structure ?

Answer 14

The H-bond interactions

Question 15

How many amino acid residues are found per turn of helix ?

Answer 15

3.6

Question 16

Where do Gly & Pro residues occur ?

Answer 16

In the B-turns on the surface of globular proteins.