Study of the dynamics of protein folding through minimalistic models

 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. Received: 28 April 2002 / Accepted: 11 August 2002 / Published online: 13 November 2002 Correspondence to: B. Bagchi e-mail: bbagchi@sscu.iisc.ernet.in Acknowledgements. We thank Samir Pal and Arnab Mukherjee for many discussions and Arun Yethiraj for helpful suggestions. The financial support from DST, India, is gratefully acknowledged. G. S. thanks CSIR for a research fellowship.