Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1979803 | Current Opinion in Structural Biology | 2007 | 6 Pages |
Abstract
The Helmholtz free energy, F, plays an important role in proteins because of their rugged potential energy surface, which is ‘decorated’ with a tremendous number of local wells (denoted microstates, m). F governs protein folding, whereas differences ΔFmn determine the relative populations of microstates that are visited by a flexible cyclic peptide or a flexible protein segment (e.g. a surface loop). Recently developed methodologies for calculating ΔFmn (and entropy differences, ΔSmn) mainly use thermodynamic integration and calculation of the absolute F; interesting new approaches in these categories are the adaptive integration method and the hypothetical scanning molecular dynamics method, respectively.
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Authors
Hagai Meirovitch,