| Evolution of physics-based methodology for exploring the conformational energy landscape of proteins |
| Harold A. Scheraga 1 *, Jaroslaw Pillardy 1, Adam Liwo 1 2, Jooyoung Lee 1, Cezary Czaplewski 1 2, Daniel R. Ripoll 3, William J. Wedemeyer 1 4, Yelena A. Arnautova 1 |
| 1Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301 2Department of Chemistry, University of Gdansk, Gdansk, Poland 3Cornell Theory Center, Cornell University, Ithaca, NY 14853-3801 4National Institutes of Health Postdoctoral Fellow |
| email: Harold A. Scheraga (has5@cornell.edu) |
*Correspondence to Harold A. Scheraga, Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301
Funded by:
National Institutes of Health; Grant Number: GM-14312
National Science Foundation; Grant Number: MCB95-13167
Fogarty Foundation; Grant Number: TW1064
NIH National Center for Research Resources; Grant Number: P41RR-04293
Polish State Committee for Scientific Research, KBN; Grant Number: 3 T09A 111 17, 127/E-335/S/2000
National Foundation for Cancer Research
| Keywords |
| physics-based methodology; protein conformation; protein folding |
| Abstract |
| The evolution of our physics-based computational methods for determining protein conformation without the introduction of secondary-structure predictions, homology modeling, threading, or fragment coupling is described. Initial use of a hard-sphere potential captured much of the structural properties of polypeptide chains, and subsequent more refined force fields, together with efficient methods of global optimization provide indications that progress is being made toward an understanding of the interresidue interactions that underlie protein folding. © 2002 John Wiley & Sons, Inc. J Comput Chem 23: 28-34, 2002 |
| Digital Object Identifier (DOI) |