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Electrostatic interactions in aromatic oligopeptides contribute to protein stability |
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| Authors: | Stephen K. Burley Gregory A. Petsko |
| Affiliation: | a Department of Chemistry, Harvard University, Cambridge, MA 02138, USA b Department of Medicine, Brigham and Women's Hospital, 75 Francis Street, Boston, MA 02115, USA c Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA |
| Abstract: | Recent X-ray crystallographic studies of aromatic oligopeptides have shown that aromatic amino acid side chains participate in enthalpically-favorable, weakly polar interactions that stabilize oligopeptide folds. These interactions are important in peptides used as model therapeutic agents for sickle-cell disease, in vasopressin (antidiuretic hormone) and in [Leu]-enkephalin. The aromatic groups of globular proteins display similar behavior and thereby contribute to the stability of the three-dimensional structure of proteins. |
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