Proportion of solvent-exposed amino acids in a protein and rate of protein evolution

Yeong-Shin Lin*, Wei Lun Hsu, Jenn Kang Hwang, Wen Hsiung Li

*Corresponding author for this work

Research output: Contribution to journalArticle

70 Scopus citations


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 (P exposed ) can reach two-thirds of that explained by translational selection, indicating that P exposed 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.

Original languageEnglish
Pages (from-to)1005-1011
Number of pages7
JournalMolecular Biology and Evolution
Issue number4
StatePublished - 1 Apr 2007


  • Disordered
  • Evolutionary rate
  • Fitness density
  • Functional density
  • Protein structure
  • Solvent accessibility

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