Solvent effects on conformational stability of peptides: RISM analyses

We describe features of our methodology for predicting tertiary structures (i.e., conformations) of proteins in solvent just from the amino-acid seque nces and molecular models for the solvent. The methodology, which is a comb ination of the Monte Carlo simulated annealing technique and the reference interaction site model theory, is illustrated for the small peptides, Met-e nkephalin and C-peptide. Important roles played by water are discussed, and the alcohol effects on peptide conformations are newly analyzed. (C) 2001 Elsevier Science B.V. All rights reserved.