Solvent-induced organization: A physical model of folding myoglobin

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dc.creatorCallaway, David J. E.
dc.date1994-06-16
dc.date.accessioned2026-07-07T03:07:18Z
dc.date.available2026-07-07T03:07:18Z
dc.descriptionThe 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.
dc.descriptionRockefeller preprint RU 93-3-B 28 pages, plain LATEX Figures available by request to climber@summit.rockefeller.edu
dc.identifierhttps://arxiv.org/abs/cond-mat/9406071
dc.identifierhttp://arxiv.org/abs/cond-mat/9406071
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/27122
dc.subjectCondensed Matter
dc.subjectChemical Physics
dc.subjectHigh Energy Physics - Lattice
dc.subjectQuantitative Biology
dc.titleSolvent-induced organization: A physical model of folding myoglobin
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