Solvent‐induced organization: A physical model of folding myoglobin | Zendy

Callaway David J. E. | Zendy

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Solvent‐induced organization: A physical model of folding myoglobin

Author(s) -

Callaway David J. E.

Publication year - 1994

Publication title -

proteins: structure, function, and bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.699

H-Index - 191

eISSN - 1097-0134

pISSN - 0887-3585

DOI - 10.1002/prot.340200203

Subject(s) - myoglobin , folding (dsp implementation) , chemistry , protein folding , leghemoglobin , hemeprotein , solvent , chemical physics , biophysics , biological system , computational chemistry , heme , biochemistry , organic chemistry , biology , engineering , electrical engineering , enzyme , root nodule , nitrogen fixation , nitrogen

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. © 1994 Wiley‐Liss, Inc.

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