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protein folding
The post-translational process of folding proteins into their biologically active conformations.
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)
Structure:
- see protein structure
Related
foldapathy
protein structure
General
biochemistry
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: 15299042
- Komaroff AL
Breakthrough Discovery in Protein Structure Prediction and the
Promise of New Treatments.
JAMA. Published online September 23, 2021.
PMID: 34554183
https://jamanetwork.com/journals/jama/fullarticle/2784583