title: Models for protein folding and nature's choice of protein as catalyst.
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.
authors.affiliation: Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, 202002, India. rizwanhkhan@hotmail.com
authors.forename: R H
authors.initials: RH
authors.lastname: Khan
authors.forename: F
authors.initials: F
authors.lastname: Khan
mesh_terms: D002384:Catalysis; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D004798:Enzymes