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MBE Advance Access originally published online on January 29, 2007
Molecular Biology and Evolution 2007 24(4):1005-1011; doi:10.1093/molbev/msm019
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© The Author 2007. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Research Articles

Proportion of Solvent-Exposed Amino Acids in a Protein and Rate of Protein Evolution

Yeong-Shin Lin*,{dagger}, Wei-Lun Hsu{ddagger}, Jenn-Kang Hwang*,{ddagger} and Wen-Hsiung Li{dagger}

* Department of Biological Science and Technology, National Chiao Tung University, Hsinchu, Taiwan
{dagger} Department of Ecology and Evolution, University of Chicago
{ddagger} Institute of Bioinformatics, National Chiao Tung University, Hsinchu, Taiwan

E-mail: whli{at}uchicago.edu.

Accepted for publication January 22, 2007.

Translational selection, including gene expression, protein abundance, and codon usage bias, has been suggested as the single dominant determinant of protein evolutionary rate in yeast. Here, we show that protein structure is also an important determinant. Buried residues, which are responsible for maintaining protein structure or are located on a stable interaction surface between 2 subunits, are usually under stronger evolutionary constraints than solvent-exposed residues. Our partial correlation analysis shows that, when whole proteins are included, the variance of evolutionary rate explained by the proportion of solvent-exposed residues (Pexposed) can reach two-thirds of that explained by translational selection, indicating that Pexposed is the most important determinant of protein evolutionary rate next only to translational selection. Our result suggests that proteins with many residues under selective constraint (e.g., maintaining structure or intermolecular interaction) tend to evolve slowly, supporting the "fitness (functional) density" hypothesis.

Key Words: evolutionary rate • protein structure • fitness density • functional density • solvent accessibility • disordered


William Martin, Associate Editor


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E. A. Franzosa and Y. Xia
Structural Determinants of Protein Evolution Are Context-Sensitive at the Residue Level
Mol. Biol. Evol., October 1, 2009; 26(10): 2387 - 2395.
[Abstract] [Full Text] [PDF]



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