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Molecular chaperones in cellular protein folding

✍ Scribed by Jörg Martin; F.-Ulrich Hartl

Publisher
John Wiley and Sons
Year
1994
Tongue
English
Weight
691 KB
Volume
16
Category
Article
ISSN
0265-9247

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✦ Synopsis

Abstract

The discovery of “molecular chaperones” 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. Understanding the structure and function of molecular chaperones is likely to yield useful applications for medicine and biotechnology in the future.

📜 SIMILAR VOLUMES

Protein chaperones and protein folding
Protein chaperones and protein folding
✍ Hiram F. Gilbert 📂 Article 📅 1994 🏛 Elsevier Science 🌐 English ⚖ 547 KB

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,