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Science 30 August 1985:
Vol. 229. no. 4716, pp. 834 - 838
DOI: 10.1126/science.4023714
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Articles

Science, Vol 229, Issue 4716, 834-838
Copyright © 1985 by American Association for the Advancement of Science

articles

Hydrophobicity of amino acid residues in globular proteins

GD Rose, AR Geselowitz, GJ Lesser, RH Lee, and MH Zehfus

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.


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