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Mutation matrices and physical-chemical properties: Correlations and implications by Jeffrey M. Koshi; Richard A. Goldstein is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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To investigate how the properties of individual amino acids result in proteins with particular structures and functions, we have examined the correlations between previously derived structure-dependent mutation rates and changes in various physicalchemical properties of the amino acids such as volume, charge, a-helical and b-sheet propensity, and hydrophobicity. In most cases we found the DG of transfer from octanol to water to be the best model for evolutionary constraints, in contrast to the much weaker correlation with the DG of transfer from cyclohexane to water, a property found to be highly correlated to changes in stability in sitedirected mutagenesis studies. This suggests that natural evolution may follow different rules than those suggested by results obtained in the laboratory. A high degree of conservation of a surface residue's relative hydrophobicity was also observed, a fact that cannot be explained by constraints on protein stability but that may reflect the consequences of the reverse-hydrophobic effect. Local propensity, especially a-helical propensity, is rather poorly conserved during evolution, indicating that non-local interactions dominate protein structure f

Who reads Mutation matrices and physical-chemical properties: Correlations and implications?

Author

Jeffrey M. Koshi; Richard A. Goldstein

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

1997

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)