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Structure-based statistical thermodynamic analysis of T4 lysozyme mutants: structural mapping of cooperative interactions by Vincent J. Hilser; Benjamin D. Townsend; Ernesto Freire is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The recent development of a strnctural parameterization of the energetics of protein folding has permitted the incorporation of the functions that describe the enthalpy, entropy and heat capacity changes, i.e. the individual components of the Gibbs energy, into a statistical thermodynamic formalism that describes the distribution of conformational states under equilibrium conditions. The goal of this approach is to construct with the computer a large ensemble of conformational states, and then to derive the most probable population distribution, i.e. the distribution of states that best accounts for a wide array of experimental observables. This analysis has been applied to four different mutants of T4 lysozyme (S44A. S44G, V131A, V131G). It is shown that the structural parameterization predicts well the stability of the protein and the effects of the mutations. The entire set of folding constants per residue has been calculated for the four mutants. In all cases, the effect of the mutations propagates beyond the mutation site itself through sequence and three-dimensional space. This phenomenon occurs despite the fact that the mutations are at solvent-exposed locations and do not d

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Author

Vincent J. Hilser; Benjamin D. Townsend; Ernesto Freire

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0301-4622)

Published

1997

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)