Peptide models XXXIV. Side-chain conformational potential energy surfaces associated with all major backbone folds of neutral tautomers of N- and C-protected L-histidine. An ab initio study on ethylimidazole and N-formyl-L-histidinamide

Péter Hudáky, Tamás Beke, András Perczel

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Abstract

Both tautomers of N-formyl-L-histidinamide and ethylimidazole were subjected to conformational analysis at the ab initio RHF/6-31G(d) level of theory. Side-chain potential energy surfaces (PES) were calculated for the nine typical backbone conformations predicted by Multidimensional Conformational Analysis. The side-chain torsions of N-formyl-L-histidinamide (X1 and X2) were characterized with respect to the shapes of the PES. All envisaged minima were fully optimized. For each conformer of N-formyl-L-histidinamide stabilization energy was calculated and compared to values determined for other amino acid residues.

Original languageEnglish
Pages (from-to)117-135
Number of pages19
JournalJournal of Molecular Structure: THEOCHEM
Volume583
Issue number1-3
DOIs
Publication statusPublished - Apr 19 2002

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Keywords

  • Ab initio
  • Conformation analysis
  • Ethylimidazole
  • Histidine
  • Potential energy surface

ASJC Scopus subject areas

  • Biochemistry
  • Condensed Matter Physics
  • Physical and Theoretical Chemistry

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