2026-07-072026-07-07http://salesiana.dossiersoluciones.com/handle/123456789/27122The 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.Rockefeller preprint RU 93-3-B 28 pages, plain LATEX Figures available by request to climber@summit.rockefeller.eduCondensed MatterChemical PhysicsHigh Energy Physics - LatticeQuantitative Biologytext