Comparative study of global minimum energy conformations of hydrated peptides

A global optimization method is described for identifying the global minimu m energy conformation, as well as lower and upper bounds on the global mini mum conformer of solvated peptides. Ln 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, whe reas the second method uses information on the solvent-accessible volume of hydration shells. The hydration effects predicted by the area- and volume- based models, using a variety of atomic solvation parameter (ASP) sets, are tested and compared by identifying global minimum energy structures of ter minally blocked peptides and oligopeptides. Significant differences are obs erved, indicating that appropriate model selection is essential for accurat ely predicting hydrated peptide structures. Using this information, the app licability of these hydration models and ASP sets is discussed. (C) 1999 Jo hn Wiley & Sons, Inc.