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, A. Perczel

Research output: Contribution to journalArticle

11 Citations (Scopus)

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
DOIs
Publication statusPublished - Apr 19 2002

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Potential energy surfaces
histidine
tautomers
Histidine
Peptides
peptides
potential energy
Amino Acids
Torsional stress
torsion
amino acids
Conformations
Amino acids
Stabilization
stabilization
energy

Keywords

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

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Computational Theory and Mathematics
  • Atomic and Molecular Physics, and Optics

Cite this

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title = "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",
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.",
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author = "P{\'e}ter Hud{\'a}ky and Tam{\'a}s Beke and A. Perczel",
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T1 - 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

AU - Hudáky, Péter

AU - Beke, Tamás

AU - Perczel, A.

PY - 2002/4/19

Y1 - 2002/4/19

N2 - 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.

AB - 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.

KW - Ab initio

KW - Conformation analysis

KW - Ethylimidazole

KW - Histidine

KW - Potential energy surface

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DO - 10.1016/S0166-1280(01)00804-1

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VL - 583

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JO - Computational and Theoretical Chemistry

JF - Computational and Theoretical Chemistry

SN - 2210-271X

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