title: Conformational analysis of the tyrosine dipeptide analogue in the gas phase and in aqueous solution by a density functional/continuum solvent model.
abstract: 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.
authors.affiliation: Dipartimento di Chimica, Università Federico II, Napoli, Italy.
authors.forename: Emma
authors.initials: E
authors.lastname: Langella
authors.forename: Nadia
authors.initials: N
authors.lastname: Rega
authors.forename: Roberto
authors.initials: R
authors.lastname: Improta
authors.forename: Orlando
authors.initials: O
authors.lastname: Crescenzi
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Barone
mesh_terms: D000465:Algorithms; D004151:Dipeptides / Q000737:chemistry*; D008956:Models, Chemical; D008968:Molecular Conformation; D012996:Solutions; D012997:Solvents; D014443:Tyrosine / Q000737:chemistry*
chemical_list: D004151:Dipeptides; D012996:Solutions; D012997:Solvents; D014443:Tyrosine