Peptide models XXXV. Protonated and deprotonated N-formyl-L-histidinamide: An ab initio study on side-chain potential energy surfaces of all major backbone conformers

Péter Hudáky, Ilona Hudáky, András Perczel

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Charged forms of N-Formyl-L-histidinamide and ethylimidazole molecules were subjected to conformational analysis at the ab initio RHF/6-31G(d) level of theory. Side-chain potential energy surfaces, E = Ebb(X1,X2), were calculated at the nine typical backbone conformations (bb = αL, αD, βL, γL, γD, δL, δD, εL and εD) given by multidimensional conformational analysis (MDCA). Envisaged minima obtained from the topological analysis of E = Ebb(X1,X2) surfaces and from MDCA were fully optimized. Electrostatic interaction between charged side-chain and polar peptide bonds is discussed. Stabilization energy was calculated for each conformer of N-Formyl-L-histidinamide and scored relative to the stabilization energy of other amino acids.

Original languageEnglish
Pages (from-to)199-213
Number of pages15
JournalJournal of Molecular Structure: THEOCHEM
Volume583
Issue number1-3
DOIs
Publication statusPublished - Apr 19 2002

Keywords

  • Ab initio
  • Conformation
  • Ethylimidazole
  • Histidine
  • Side-chain potential energy surface
  • pH

ASJC Scopus subject areas

  • Biochemistry
  • Condensed Matter Physics
  • Physical and Theoretical Chemistry

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