Article ID Journal Published Year Pages File Type
1979803 Current Opinion in Structural Biology 2007 6 Pages PDF
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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Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
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