Počet záznamů: 1

The DF-LCCSD(T0) correction of the .fi./.psi. force field dihedral parameters significantly influences the free energy profile of the alanine dipeptide

  1. 1.
    0369287 - UOCHB-X 2012 RIV NL eng J - Článek v odborném periodiku
    Vymětal, Jiří - Vondrášek, Jiří
    The DF-LCCSD(T0) correction of the .fi./.psi. force field dihedral parameters significantly influences the free energy profile of the alanine dipeptide.
    Chemical Physics Letters. Roč. 503, 4/6 (2011), s. 301-304 ISSN 0009-2614
    Grant CEP: GA ČR GAP208/10/0725; GA MŠk LC512; GA MŠk(CZ) LH11020
    Výzkumný záměr: CEZ:AV0Z40550506
    Klíčová slova: conformational preferences * quantum-mechanics * gas-phase * simulations * peptides
    Kód oboru RIV: CF - Fyzikální chemie a teoretická chemie
    Impakt faktor: 2.337, rok: 2011

    The conformational behavior of small peptides is mostly dictated by backbone rigidity, in which the phi/psi torsions seem to play the most important role. We show that ab initio-based corrections of the torsion parameters in the FF-FOM force field determined by the DF-LCCSD(T0) method significantly influence the quality and minimum localization on the 2D free energy surface of the alanine dipeptide (AD) along the phi and psi coordinates of the backbone torsion angles. The populations of the individual conformers are in good agreement with the experimental results published recently on the AD through an analysis of the amide III band and the Raman skeletal vibrations. (C) 2011 Elsevier B.V. All rights reserved.
    Trvalý link: http://hdl.handle.net/11104/0006738