Journal
JOURNAL OF COMPUTATIONAL CHEMISTRY
Volume 25, Issue 11, Pages 1333-1341Publisher
WILEY
DOI: 10.1002/jcc.20062
Keywords
dipeptide analog; helical conformers; density functionals; noncovalent interactions
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The role of intraresidue interactions in determining the conformational behavior of polypeptides is analyzed by means of density functional and post-Hartree-Fock computations on the alanine dipeptide analog and other model compounds. Our computations show that the accuracy of current density functionals is sufficient for H-bond, electrostatic, inductive, and short-range repulsive interactions, whereas medium-range attractions between electron-rich atoms and/or bonds are underestimated. This leads, in turn, to an underestimation of the stability of helical structures w.r.t. extended or folded conformers involving H-bonds. Those results could pave the route for devising local ad hoc corrections able to significantly improve structural and dynamic predictions for polypeptides issuing from DFT computations. (C) 2004 Wiley Periodicals, Inc.
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