✦ LIBER ✦

Protein folding in vitro

✍ Scribed by Kunihiro Kuwajima

Publisher: Elsevier Science
Year: 1992
Tongue: English
Weight: 732 KB
Volume: 3
Category: Article
ISSN: 0958-1669
DOI: 10.1016/0958-1669(92)90072-q

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✦ Synopsis

It is becoming increasingly evident that intermediates observed in protein folding in vitro may be closely related to conformational states that are important in various intracellular processes. This review focuses on recent advances in in vitro protein-folding studies with particular reference to the molten globule state, which is purported to be a common and distinct intermediate of protein folding.

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## Abstract Proteolytic dissection of native __trp__ repressor and horse heart cytochrome __c__ has been used to infer some of the steps in the folding pathways of the intact proteins. For both proteins, small fragments are capable of undergoing spontaneous noncovalent association to form subdomain