The conformational behavior of a tyrosine dipeptide analog, MeCO-Tyr-NHMe, has been investigated by d. functional methods using the polarizable continuum model (PCM) for the description of solvent effects. This study points out the interplay of backbone and side chain contributions in detg. the relative stabilities of energy min. In particular, stabilizing interactions between the NH bond and the arom. ring have a significant effect. The topol. of the potential energy surface is significantly modified in aq. soln. due to a general widening of low energy regions and to a stabilization of helical structures.
Conformational analysis of the tyrosine dipeptide analogue in the gas phase and in aqueous solution by a density functional/continuum solvent model
Langella E;Improta R;
2002
Abstract
The conformational behavior of a tyrosine dipeptide analog, MeCO-Tyr-NHMe, has been investigated by d. functional methods using the polarizable continuum model (PCM) for the description of solvent effects. This study points out the interplay of backbone and side chain contributions in detg. the relative stabilities of energy min. In particular, stabilizing interactions between the NH bond and the arom. ring have a significant effect. The topol. of the potential energy surface is significantly modified in aq. soln. due to a general widening of low energy regions and to a stabilization of helical structures.File in questo prodotto:
Non ci sono file associati a questo prodotto.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
