Peptide models XXIV: An ab initio study on N-formyl-L-prolinamide with trans peptide bond. The existence or non-existence of α(L) and ε(L) conformations

Hector A. Baldoni, Ana M. Rodriguez, Miguel A. Zamora, Graciela N. Zamarbide, Ricardo D. Enriz, Ödön Farkas, Pal Csàszàr, Ladislaus L. Torday, Carlos P. Sosa, Imre Jàkli, Andràs Perzel, Julius Gy Papp, Miklos Hollosi, Imre G. Csizmadia

Research output: Contribution to journalArticle

53 Citations (Scopus)

Abstract

N-formyl-L-prolinamide was subjected to geometry optimization at three levels of theory: HF/3-21G, HF/6-31G (d) and B3LYP/6-31G (d). At all three levels of computation the global minimum was γ(L) (inverse γ-Turn) backbone conformation with two ring-puckered forms 'UP' and 'DOWN'. At HF/3-21G level of theory three backbone conformations were found γ(L), ε(L), and α(L). At higher levels of theory the ε(L), and α(L) conformations disappeared. The 'UP' and 'DOWN' ring-puckered forms, in the γ(L) backbone conformation, led to practically identical vibrational spectra at the B3LYP/6-31G (d) level of theory.

Original languageEnglish
Pages (from-to)79-91
Number of pages13
JournalJournal of Molecular Structure: THEOCHEM
Volume465
Issue number1
DOIs
Publication statusPublished - May 31 1999

Keywords

  • Molecular conformations
  • N-formyl-L-prolinamide
  • Trans-Peptide bond

ASJC Scopus subject areas

  • Biochemistry
  • Condensed Matter Physics
  • Physical and Theoretical Chemistry

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