Literature DB >> 16901983

Systematically assessing the influence of 3-dimensional structural context on the molecular evolution of mammalian proteomes.

Sun Shim Choi1, Eric J Vallender, Bruce T Lahn.   

Abstract

The 3-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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Year:  2006        PMID: 16901983     DOI: 10.1093/molbev/msl086

Source DB:  PubMed          Journal:  Mol Biol Evol        ISSN: 0737-4038            Impact factor:   16.240


  16 in total

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6.  Structural mapping of protein interactions reveals differences in evolutionary pressures correlated to mRNA level and protein abundance.

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7.  Independent effects of protein core size and expression on residue-level structure-evolution relationships.

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8.  A model for protein sequence evolution based on selective pressure for protein stability: application to hemoglobins.

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9.  Quantitative residue-level structure-evolution relationships in the yeast membrane proteome.

Authors:  Eric A Franzosa; Ran Xue; Yu Xia
Journal:  Genome Biol Evol       Date:  2013       Impact factor: 3.416

10.  A conserved mammalian protein interaction network.

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Journal:  PLoS One       Date:  2013-01-02       Impact factor: 3.240

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