1994/06/16 by David J.E. Callaway, David J. E. Callaway, Callaway, David J. E.
Biochemistry, Genetics and Molecular Biology · Physics and Astronomy · #Hemoglobin structure and function #Protein Interaction Studies and Fluorescence Analysis #Protein Structure and Dynamics #chem-ph #cond-mat #hep-lat #q-bio
paper · pdf · doi:10.48550/arxiv.cond-mat/9406071
Rockefeller preprint RU 93-3-B 28 pages, plain LATEX Figures available by request to [email protected]
arxiv created 1994/06/16 · arxiv updated 2009/11/30
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.