Chapter 2

Flashcards highlighting key vocabulary and concepts related to protein folding and the role of molecular chaperones.

hydrophobic regions

• nonpolar

• aggregation → misfoling

Molecular chaperones

Proteins that assist in the folding of other proteins and prevent misfolding and aggregation.

Hsp70 family

• molecular chaperones that help proteins refold,

• stress conditions like heat shock.

Chaperonins

• A class of chaperones that provide an isolated environment for proteins to fold

• GroEL and TRiC.

GroEL

• A bacterial chaperonin composed of 14 polypeptides that assists in protein folding.

GroES

• A co-chaperonin that binds to GroEL, enhancing its ability to facilitate proper protein folding.

• “cap”

what happens when GreES binds to GroEL

• chamber expands → hydrophilic

• requires ATP hydrolysis

• proper folding environment

Aggregates

Clusters of misfolded proteins that can cause cellular dysfunction and diseases.

Protein folding diseases

• Alzheimer's

• Parkinson's

• Huntington's disease

• cystic fibrosis

α-helix to β-sheet transition

• protein folding diseases

• normal helix structure converts to a sheet structure, leading to aggregation.

Heat shock response

• A protective mechanism activated in cells that causes the upregulation of chaperones and other proteins in response to stress, such as heat.

which chaperone molecule operates co-translationally

Hsp70

which chaperonin has a hydrophobic chamber

GroEL

which chaperonin changes hydrophobic → hydrophilic

GroES

dimerization and oligomerization

• lead to higher order aggregates