REVIEW: Models for Protein Folding and Nature's Choice of Protein as Catalyst

R. H. Khan^* and F. Khan

Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202002, India; fax: 91-571-701081; E-mail: rizwanhkhan@hotmail.com

^* To whom correspondence should be addressed.

Received June 19, 2001; Revision received August 28, 2001

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The study of protein folding and unfolding pathways lends a fascinating dimension to protein biochemistry. Several models for protein folding have been postulated. Two powerful probes used in protein folding study are far UV-CD monitored stopped flow kinetics and pulse hydrogen exchange in conjunction with NMR. The formation of molten globule, which is an intermediate possessing secondary structure but not a well packed tertiary structure, is now emerging as a common feature on the folding pathway of many proteins. The molten globule is recognized by a class of molecules called chaperones which act as accelerators of protein folding. This article ends by elucidating why proteins are Nature's choice as catalysts.

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KEY WORDS: protein folding, molten globule, biocatalysis

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