Literature DB >> 12059770

Models for protein folding and nature's choice of protein as catalyst.

R H Khan1, F Khan.   

Abstract

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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Year:  2002        PMID: 12059770     DOI: 10.1023/a:1015537909889

Source DB:  PubMed          Journal:  Biochemistry (Mosc)        ISSN: 0006-2979            Impact factor:   2.487


  2 in total

Review 1.  Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.

Authors:  Vijay M Krishnamurthy; George K Kaufman; Adam R Urbach; Irina Gitlin; Katherine L Gudiksen; Douglas B Weibel; George M Whitesides
Journal:  Chem Rev       Date:  2008-03       Impact factor: 60.622

2.  Functional refolding of the Campylobacter jejuni MOMP (major outer membrane protein) porin by GroEL from the same species.

Authors:  Florence Goulhen; Emmanuelle Dé; Jean-Marie Pagès; Jean-Michel Bolla
Journal:  Biochem J       Date:  2004-03-15       Impact factor: 3.857

  2 in total

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