Theoretical studies of protein-folding thermodynamics and kinetics
Recently, protein-folding models have advanced to the point where folding simulations of protein-like chains of reasonable length (up to 125 amino acids) are feasible, and the major physical features of folding proteins, such as cooperativity in thermodynamics and nucleation mechanisms in kinetics,...
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Veröffentlicht in: | Current opinion in structural biology 1997-02, Vol.7 (1), p.29-40 |
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Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: | Recently, protein-folding models have advanced to the point where folding simulations of protein-like chains of reasonable length (up to 125 amino acids) are feasible, and the major physical features of folding proteins, such as cooperativity in thermodynamics and nucleation mechanisms in kinetics, can be reproduced. This has allowed deep insight into the physical mechanism of folding, including the solution of the so-called ‘Levinthal paradox’. |
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ISSN: | 0959-440X 1879-033X |
DOI: | 10.1016/S0959-440X(97)80005-X |