• DOI:10.1126/SCIENCE.4023714
• Corpus ID: 22227053

Hydrophobicity of amino acid residues in globular proteins.

@article{Rose1985HydrophobicityOA,
  title={Hydrophobicity of amino acid residues in globular proteins.},
  author={George D. Rose and A R Geselowitz and Glenn J. Lesser and R H Lee and Micheal H. Zehfus},
  journal={Science},
  year={1985},
  volume={229 4716},
  pages={
          834-8
        }
}

• G. Rose, A. R. Geselowitz, +2 authors M. H. Zehfus
• Published 30 August 1985
• Biology
• Science

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.