protein folding
Jump to navigation
Jump to search
Introduction
The post-translational process of folding proteins into their biologically active conformations.
Structure
Biochemistry
- unfolded or misfold proteins have exposed hydrophobic regions that render them prone to aggregation
- to avoid this, molecular chaperones bind to them to keep them soluble either until they reach their destination or are degraded by cellular proteases (ubiquitin-proteasome system)
More general terms
Additional terms
References
- ↑ Giffard RG, Xu L, Zhao H, Carrico W, Ouyang Y, Qiao Y, Sapolsky R, Steinberg G, Hu B, Yenari MA. Chaperones, protein aggregation, and brain protection from hypoxic/ischemic injury. J Exp Biol. 2004 Aug;207(Pt 18):3213-20. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/15299042
- ↑ Komaroff AL Breakthrough Discovery in Protein Structure Prediction and the Promise of New Treatments. JAMA. Published online September 23, 2021. PMID: https://www.ncbi.nlm.nih.gov/pubmed/34554183 https://jamanetwork.com/journals/jama/fullarticle/2784583