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, A. Perczel

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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
DOIs
Publication statusPublished - Apr 19 2002

Fingerprint

Potential energy surfaces
Static Electricity
Peptides
peptides
Stabilization
stabilization
potential energy
Amino Acids
Coulomb interactions
amino acids
Conformations
Amino acids
electrostatics
Molecules
energy
molecules
interactions

Keywords

  • Ab initio
  • Conformation
  • Ethylimidazole
  • Histidine
  • pH
  • Side-chain 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 XXXV. Protonated and deprotonated N-formyl-L-histidinamide: An ab initio study on side-chain potential energy surfaces of all major backbone conformers",
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.",
keywords = "Ab initio, Conformation, Ethylimidazole, Histidine, pH, Side-chain potential energy surface",
author = "P{\'e}ter Hud{\'a}ky and Ilona Hud{\'a}ky and A. Perczel",
year = "2002",
month = "4",
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language = "English",
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journal = "Computational and Theoretical Chemistry",
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T1 - Peptide models XXXV. Protonated and deprotonated N-formyl-L-histidinamide

T2 - An ab initio study on side-chain potential energy surfaces of all major backbone conformers

AU - Hudáky, Péter

AU - Hudáky, Ilona

AU - Perczel, A.

PY - 2002/4/19

Y1 - 2002/4/19

N2 - 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.

AB - 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.

KW - Ab initio

KW - Conformation

KW - Ethylimidazole

KW - Histidine

KW - pH

KW - Side-chain potential energy surface

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U2 - 10.1016/S0166-1280(01)00812-0

DO - 10.1016/S0166-1280(01)00812-0

M3 - Article

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VL - 583

SP - 199

EP - 213

JO - Computational and Theoretical Chemistry

JF - Computational and Theoretical Chemistry

SN - 2210-271X

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