Molecular orbital analysis of the effect of D- and L-alanyl residues on the glycine chirality within the tripeptide N-Ac-Ala-Gly[β]-Ala-NH-Me. An ab initio and DFT study

Jack C C Liao, Gregory A. Chass, David H. Setiadi, I. Csizmadia

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

A conformational analysis of the tripeptide models, N-Ac-D-Ala-Gly[β]- L-Ala-NH-Me and N-Ac-L-Ala-Gly[β]-L-Ala-NH-Me, was carried out using ab initio Molecular Orbital (MO) computations at the RHF/6-31G(d) and B3LYP/6-31G(d) levels of theory. At both levels of theory, global and local minima on the Ramachandran potential energy surfaces (PES), E=f(φ 11) and E=f(φ33), of the two systems associated with the possible 18 backbone orientations were geometries optimized. When a glycyl residue was sandwiched between two chiral amino acids such as alanyl residues, its Cα-HR and Cα-HS bond lengths were no longer equal but instead perturbed slightly; inducing a chirality on the glycyl residue. Depending on the respective conformations of the adjacent alanyl residues, the magnitude of the conformational impact was investigated in this article.

Original languageEnglish
Pages (from-to)321-326
Number of pages6
JournalJournal of Molecular Structure: THEOCHEM
Volume666-667
DOIs
Publication statusPublished - Dec 29 2003

Fingerprint

alanylglycine
Potential energy surfaces
Chirality
Bond length
Molecular orbitals
glycine
chirality
Discrete Fourier transforms
Glycine
Conformations
Amino acids
molecular orbitals
Molecular Computers
Amino Acids
Geometry
amino acids
potential energy
geometry

Keywords

  • Ab initio molecular orbital computations
  • Alanyl residue
  • Chiral induction on glycine α carbon
  • Conformational potential energy surfaces
  • Glycyl residue
  • Multidimensional conformational analysis
  • N-Ac-D-Ala-Gly-L-Ala-NH-Me
  • N-Ac-L-Ala-Gly-L-Ala-NH-Me

ASJC Scopus subject areas

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

Cite this

Molecular orbital analysis of the effect of D- and L-alanyl residues on the glycine chirality within the tripeptide N-Ac-Ala-Gly[β]-Ala-NH-Me. An ab initio and DFT study. / Liao, Jack C C; Chass, Gregory A.; Setiadi, David H.; Csizmadia, I.

In: Journal of Molecular Structure: THEOCHEM, Vol. 666-667, 29.12.2003, p. 321-326.

Research output: Contribution to journalArticle

@article{77ceae4c21df47439e1476f9e1703bde,
title = "Molecular orbital analysis of the effect of D- and L-alanyl residues on the glycine chirality within the tripeptide N-Ac-Ala-Gly[β]-Ala-NH-Me. An ab initio and DFT study",
abstract = "A conformational analysis of the tripeptide models, N-Ac-D-Ala-Gly[β]- L-Ala-NH-Me and N-Ac-L-Ala-Gly[β]-L-Ala-NH-Me, was carried out using ab initio Molecular Orbital (MO) computations at the RHF/6-31G(d) and B3LYP/6-31G(d) levels of theory. At both levels of theory, global and local minima on the Ramachandran potential energy surfaces (PES), E=f(φ 1,ψ1) and E=f(φ3,ψ3), of the two systems associated with the possible 18 backbone orientations were geometries optimized. When a glycyl residue was sandwiched between two chiral amino acids such as alanyl residues, its Cα-HR and Cα-HS bond lengths were no longer equal but instead perturbed slightly; inducing a chirality on the glycyl residue. Depending on the respective conformations of the adjacent alanyl residues, the magnitude of the conformational impact was investigated in this article.",
keywords = "Ab initio molecular orbital computations, Alanyl residue, Chiral induction on glycine α carbon, Conformational potential energy surfaces, Glycyl residue, Multidimensional conformational analysis, N-Ac-D-Ala-Gly-L-Ala-NH-Me, N-Ac-L-Ala-Gly-L-Ala-NH-Me",
author = "Liao, {Jack C C} and Chass, {Gregory A.} and Setiadi, {David H.} and I. Csizmadia",
year = "2003",
month = "12",
day = "29",
doi = "10.1016/j.theochem.2003.08.038",
language = "English",
volume = "666-667",
pages = "321--326",
journal = "Computational and Theoretical Chemistry",
issn = "2210-271X",
publisher = "Elsevier BV",

}

TY - JOUR

T1 - Molecular orbital analysis of the effect of D- and L-alanyl residues on the glycine chirality within the tripeptide N-Ac-Ala-Gly[β]-Ala-NH-Me. An ab initio and DFT study

AU - Liao, Jack C C

AU - Chass, Gregory A.

AU - Setiadi, David H.

AU - Csizmadia, I.

PY - 2003/12/29

Y1 - 2003/12/29

N2 - A conformational analysis of the tripeptide models, N-Ac-D-Ala-Gly[β]- L-Ala-NH-Me and N-Ac-L-Ala-Gly[β]-L-Ala-NH-Me, was carried out using ab initio Molecular Orbital (MO) computations at the RHF/6-31G(d) and B3LYP/6-31G(d) levels of theory. At both levels of theory, global and local minima on the Ramachandran potential energy surfaces (PES), E=f(φ 1,ψ1) and E=f(φ3,ψ3), of the two systems associated with the possible 18 backbone orientations were geometries optimized. When a glycyl residue was sandwiched between two chiral amino acids such as alanyl residues, its Cα-HR and Cα-HS bond lengths were no longer equal but instead perturbed slightly; inducing a chirality on the glycyl residue. Depending on the respective conformations of the adjacent alanyl residues, the magnitude of the conformational impact was investigated in this article.

AB - A conformational analysis of the tripeptide models, N-Ac-D-Ala-Gly[β]- L-Ala-NH-Me and N-Ac-L-Ala-Gly[β]-L-Ala-NH-Me, was carried out using ab initio Molecular Orbital (MO) computations at the RHF/6-31G(d) and B3LYP/6-31G(d) levels of theory. At both levels of theory, global and local minima on the Ramachandran potential energy surfaces (PES), E=f(φ 1,ψ1) and E=f(φ3,ψ3), of the two systems associated with the possible 18 backbone orientations were geometries optimized. When a glycyl residue was sandwiched between two chiral amino acids such as alanyl residues, its Cα-HR and Cα-HS bond lengths were no longer equal but instead perturbed slightly; inducing a chirality on the glycyl residue. Depending on the respective conformations of the adjacent alanyl residues, the magnitude of the conformational impact was investigated in this article.

KW - Ab initio molecular orbital computations

KW - Alanyl residue

KW - Chiral induction on glycine α carbon

KW - Conformational potential energy surfaces

KW - Glycyl residue

KW - Multidimensional conformational analysis

KW - N-Ac-D-Ala-Gly-L-Ala-NH-Me

KW - N-Ac-L-Ala-Gly-L-Ala-NH-Me

UR - http://www.scopus.com/inward/record.url?scp=1642533605&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=1642533605&partnerID=8YFLogxK

U2 - 10.1016/j.theochem.2003.08.038

DO - 10.1016/j.theochem.2003.08.038

M3 - Article

AN - SCOPUS:1642533605

VL - 666-667

SP - 321

EP - 326

JO - Computational and Theoretical Chemistry

JF - Computational and Theoretical Chemistry

SN - 2210-271X

ER -