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.
- Pub Date:
- June 1994
- Condensed Matter;
- Chemical Physics;
- High Energy Physics - Lattice;
- Quantitative Biology
- Rockefeller preprint RU 93-3-B 28 pages, plain LATEX Figures available by request to email@example.com