Chaperones and Protein Misfolding

Question 1

What are the two things PDI do? (Protein Disulfide Isomerase) when does PDI start reduced vs oxidative?

Answer 1

1. Helps the formation of the proper disulfide bonds when the disulfides are wrongly connected. (Start reduced)
2. Helps the formation of proper disulfide bonds when the disulfides are not yet formed. (Starts oxidized)

Question 2

Define what a chaperone is.

Answer 2

Proteins which assist other proteins to adopt the proper confirmation.

Question 3

What are the two types of protein chaperones we will discuss in this class? (Which one really matters) What do they do?

Answer 3

1. HSP70
2. Chaperonin GroEL/GroES.(only one we will really discuss)

Question 4

Test: fill in blanks of GroEL/GroES chaperone.

Answer 4

Question 5

How does “The GroEL/GroES chaperone: a Two-stroke Engine” work?

Answer 5

Question 6

Define Amyloids

Answer 6

Protein misfolding, forming insoluble fibrous aggregates.

Question 7

Give examples of protein misfolding disease.

Answer 7

Alzheimer’s disease: amyloid plaque consist mainly of amyloid, beta protein.
Mad cow disease : aggregates of misfolding prion protein molecules.

Question 8

Defined the characteristics of amyloid fibril.

Answer 8