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Monte Carlo determination of the internal energies of hydration for the Ala dipeptide in the C 7 , C 5 , α R , and P II conformations
Author(s) -
Mehrotra P. K.,
Mezei M.,
Beveridge D. L.
Publication year - 1984
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.560260731
Subject(s) - dipeptide , monte carlo method , chemistry , internal energy , hydration energy , computational chemistry , crystallography , chemical physics , molecule , peptide , thermodynamics , organic chemistry , physics , biochemistry , statistics , mathematics
Abstract The internal energies of hydration of the Ala dipeptide in the C 7 , C 5 , α R , and P II conformations were computed with the Monte Carlo method. The results indicate that both the α R and P II conformations are preferentially stabilized by hydration in general accord with the results of recent experiments described by Madison and Kopple. The major contributing factor for the stability of internal energy of hydration for these conformations can be traced to the hydration of the carbonyl group.