Comparative study of global minimum energy conformations of hydrated peptides

✍ Scribed by Klepeis, J. L.; Floudas, C. A.

• Publisher: John Wiley and Sons
• Year: 1999
• Tongue: English
• Weight: 320 KB
• Volume: 20
• Category: Article
• ISSN: 0192-8651
• DOI: 10.1002/(sici)1096-987x(19990430)20:6<636::aid-jcc10>3.0.co;2-d

✦ Synopsis

A global optimization method is described for identifying the global minimum energy conformation, as well as lower and upper bounds on the global minimum conformer of solvated peptides. In considering the effects of hydration, two independent continuum-based solvation models are employed. The first method is based on the calculation of solvent-accessible surface areas, whereas the second method uses information on the solvent-accessible volume of hydration shells. The hydration effects predicted by the area-and volume-Ž . based models, using a variety of atomic solvation parameter ASP sets, are tested and compared by identifying global minimum energy structures of terminally blocked peptides and oligopeptides. Significant differences are observed, indicating that appropriate model selection is essential for accurately predicting hydrated peptide structures. Using this information, the applicability of these hydration models and ASP sets is discussed.