Solvent-induced organization: A physical model of folding myoglobin
Abstract
The essential features of the in vitro refolding of myoglobin are expressed in a solvable physical model. Alpha helices are taken as the fundamental collective coordinates of the system, while the refolding is assumed to be mainly driven by solvent-induced hydrophobic forces. A quantitative model of these forces is developed and compared with experimental and theoretical results. The model is then tested by being employed in a simulation scheme designed to mimic solvent effects. Realistic dynamic trajectories of myoglobin are shown as it folds from an extended conformation to a close approximation of the native state. Various suggestive features of the process are discussed. The tenets of the model are further tested by folding the single-chain plant protein leghemoglobin.
Keywords
Cite
@article{arxiv.cond-mat/9406071,
title = {Solvent-induced organization: A physical model of folding myoglobin},
author = {David J. E. Callaway},
journal= {arXiv preprint arXiv:cond-mat/9406071},
year = {2007}
}
Comments
Rockefeller preprint RU 93-3-B 28 pages, plain LATEX Figures available by request to [email protected]