Study of the dynamics of protein folding through minimalistic models

Srinivas, Goundla and Bagchi, Biman (2003) Study of the dynamics of protein folding through minimalistic models. In: Theoretical Chemistry Accounts: Theory, Computation, and Modeling / Theoretica Chimica Acta, 109 (1). pp. 8-21.

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Abstract

Starting with the Levinthal paradox, a brief introduction to the protein folding problem is presented. The existing theories of protein folding, including the folding funnel scenario, are discussed. After briefly discussing different simulation studies of model proteins, we discuss our recent work on the dynamics of folding of the model HP-36 (the chicken villin headpiece) protein by using a simplified hydropathy scale. Special attention has been paid to the statics and dynamics of contact formation among the hydrophobic residues. The results obtained from this simple model appear to be surprisingly similar to several features observed in the folding of real proteins. The account concludes with a discussion of future problems.

Item Type:	Journal Article
Publication:	Theoretical Chemistry Accounts: Theory, Computation, and Modeling / Theoretica Chimica Acta
Publisher:	Springer
Additional Information:	Copyright of this article belongs to Springer.
Keywords:	Protein folding;Free energy;Landscape;HP-36
Department/Centre:	Division of Chemical Sciences > Solid State & Structural Chemistry Unit
Date Deposited:	24 Aug 2011 06:00
Last Modified:	24 Aug 2011 06:00
URI:	http://eprints.iisc.ac.in/id/eprint/40241

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