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MBE Advance Access published online on August 10, 2006
Molecular Biology and Evolution, doi:10.1093/molbev/msl086
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© The Author 2006. 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
Accepted August 4, 2006

Letter

Systematically Assessing the Influence of Three-Dimensional Structural Context on the Molecular Evolution of Mammalian Proteomes

Sun Shim Choi 1, Eric J. Vallender 2, and Bruce T. Lahn 1 *

1 Howard Hughes Medical Institute, Department of Human Genetics, University of Chicago, Chicago, IL 60637, USA
2 Howard Hughes Medical Institute, Department of Human Genetics, University of Chicago, Chicago, IL 60637, USA; Committee on Genetics, University of Chicago, Chicago, IL 60637, USA

* To whom correspondence should be addressed.
Bruce T. Lahn, E-mail: blahn{at}bsd.uchicago.edu


  Abstract

The three-dimensional (3D) structural context of amino acid residues in a protein could significantly impact the level of selective constraint on the residues. Here, by analyzing 767 mammalian proteins, we systematically investigate how various 3D structural contexts influence selective constraint. The structural contexts we examined include solvent accessibility, secondary structure, and intramolecular residue-residue interactions. Through this analysis, we offer quantitative information on how 3D structural contexts affect the level of selective constraint.


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