Hydrophobicity of amino acid subgroups in proteins

Glenn J. Lesser, George D. Rose

Research output: Contribution to journalArticlepeer-review

141 Scopus citations


Protein folding studies often utilize areas and volumes to assess the hydrophobic contribution to conformational free energy (Richards, F. M. Annu. Rev. Biophys. Bioeng. 6:151–176, 1977). We have calculated the mean area buried upon folding for every chemical group in each residue within a set of X‐ray elucidated proteins. These measurements, together with a standard state cavity size for each group, are documented in a table. It is observed that, on average, each type of group buries a constant fraction of its standard state area. The mean area buried by most, though not all, groups can be closely approximated by summing contributions from three characteristic parameters corresponding to three atom types: (1) carbon or sulfur, which turn out to be 86% buried, on average; (2) neutral oxygen or nitrogen, which are 40% buried, on average; and (3) charged oxygen or nitrogen, which are 32% buried, on average.

Original languageEnglish (US)
Pages (from-to)6-13
Number of pages8
JournalProteins: Structure, Function, and Bioinformatics
Issue number1
StatePublished - 1990
Externally publishedYes


  • hydrophobic effect
  • hydrophobicity
  • protein folding
  • solvent accessibility

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology


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