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Conformational analysis of the tyrosine dipeptide analogue in the gas phase and in aqueous solution by a density functional/continuum solvent model
Author(s) -
Langella Emma,
Rega Nadia,
Improta Roberto,
Crescenzi Orlando,
Barone Vincenzo
Publication year - 2002
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.10065
Subject(s) - polarizable continuum model , dipeptide , chemistry , aqueous solution , solvation , density functional theory , computational chemistry , solvent , maxima and minima , ring (chemistry) , solvent effects , chemical physics , crystallography , thermodynamics , organic chemistry , physics , amino acid , mathematics , mathematical analysis , biochemistry
The conformational behavior of a dipeptide analogue of tyrosine (TDA) has been investigated by density functional methods using the polarizable continuum model (PCM) for the description of solvent effects. Our study points out the interplay of backbone and side chain contributions in determining the relative stabilities of energy minima. In particular, stabilizing interactions between the NH bond and the aromatic ring have a significant effect. The topology of the potential energy surface is significantly modified in aqueous solution due to a general widening of low energy regions and to a stabilization of helical structures. © 2002 Wiley Periodicals, Inc. J Comput Chem 23: 650–661, 2002