Digitale Medien
New York, NY
:
Wiley-Blackwell
Proteins: Structure, Function, and Genetics
20 (1994), S. 124-138
ISSN:
0887-3585
Schlagwort(e):
leghemoglobin
;
hydrophobic
;
interactions
;
hydrophobicity
;
protein folding
;
structure prediction
;
protein dynamics
;
Chemistry
;
Biochemistry and Biotechnology
Quelle:
Wiley InterScience Backfile Collection 1832-2000
Thema:
Medizin
Notizen:
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.
Zusätzliches Material:
9 Ill.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1002/prot.340200203
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