Hydrophobicity of amino acid residues in globular proteins

George D. Rose, Ari R. Geselowitz, Glenn J. Lesser, Richard H. Lee, Micheal H. Zehfus

Research output: Contribution to journalArticlepeer-review

Abstract

During biosynthesis, a globular protein folds into a tight particle with an interior core that is shielded from the surrounding solvent. The hydrophobic effect is thought to play a key role in mediating this process: nonpolar residues expelled from water engender a molecular interior where they can be buried. Paradoxically, results of earlier quantitative analyses have suggested that the tendency for nonpolar residues to be buried within proteins is weak. However, such analyses merely classify residues as either "exposed" or "buried." In the experiment reported in this article proteins of known structure were used to measure the average area that each residue buries upon folding. This characteristic quantity, the average area buried, is correlated with residue hydrophobicity.

Original languageEnglish (US)
Pages (from-to)834-838
Number of pages5
JournalScience
Volume229
Issue number4716
DOIs
StatePublished - 1985
Externally publishedYes

ASJC Scopus subject areas

  • General

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