SOLVENT-INDUCED ORGANIZATION - A PHYSICAL MODEL OF FOLDING MYOGLOBIN

The essential features of the in vitro refolding of myoglobin are expr essed in a solvable physical model. Alpha helices are taken as the fun damental collective coordinates of the system, while the refolding is assumed to be mainly driven by solvent-induced hydrophobic forces. A q uantitative model of these forces is developed and compared with exper imental and theoretical results. The model is then tested by being emp loyed in a simulation scheme designed to mimic solvent effects. Realis tic dynamic trajectories of myoglobin are shown as it folds from an ex tended conformation to a close approximation of the native state. Vari ous suggestive features of the process are discussed. The tenets of th e model are further tested by folding the single-chain plant protein l eghemoglobin. (C) 1994 Wiley-Liss, Inc.