## Abstract The discovery of βmolecular chaperonesβ has dramatically changed our concept of cellular protein folding. Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformation in a reaction mediated by these versatile helper proteins. Und
β¦ LIBER β¦
Protein chaperones and protein folding
β Scribed by Hiram F. Gilbert
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 547 KB
- Volume
- 5
- Category
- Article
- ISSN
- 0958-1669
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β¦ Synopsis
A universal strategy for obtaining maximal protein expression or refolding remains elusive; however, headway has been made toward understanding these processes in vivo. The observation of reversible protein aggregation, asymmetry in protein--chaperone complexes, redox effects on disulfide formation, and the sequential involvement of multiple chaperones and foldases may suggest new approaches. Such new approaches include immobilized catalysts and manipulation of the bacterial periplasm.
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