Standard Article

Hydrophobic Interactions in Proteins

  1. Brian W Matthews

Published Online: 25 APR 2001

DOI: 10.1038/npg.els.0002975

eLS

eLS

How to Cite

Matthews, B. W. 2001. Hydrophobic Interactions in Proteins. eLS. .

Author Information

  1. University of Oregon, Eugene, Oregon, USA

Publication History

  1. Published Online: 25 APR 2001

Abstract

Proteins fold spontaneously into complicated three-dimensional structures that are essential for biological activity. Much of the driving energy for this folding process comes from the hydrophobic effect, i.e. the removal of nonpolar amino acids from solvent and their burial in the core of the protein.

Keywords:

  • folding;
  • non-polar;
  • water;
  • amino acid