9/6 PROTEIN REFOLDING AND DEGRADATION

Chaperone Proteins

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

Hydrophobic Interactions

Non-covalent interactions that occur between hydrophobic side chains of amino acids, driving them to cluster together away from water.

Unfolded Protein Response (UPR)

Cellular response activated to manage misfolded proteins; includes stopping protein translation and increasing chaperone production.

Proteasome

A cellular complex that degrades unneeded or damaged proteins by breaking down peptide bonds.

Lysosome

An organelle that contains enzymes for digestion of macromolecules, including proteins, and plays a critical role in degrading misfolded proteins under low pH conditions.

Ubiquitin

A small protein that tags other proteins for degradation by the proteasome.

Protein Aggregation

The accumulation of misfolded proteins in a cell, which can impair cellular function and lead to diseases.

Apoptosis

Process of programmed cell death that can be triggered when cells are overwhelmed by misfolded proteins.

Hydrophobic Environment

An environment created by chaperone proteins where misfolded proteins can refold away from water.

Energy Penalty

The cost of using molecules such as ATP for processes like protein refolding; impacts cellular economy.