Peptide models XIII. Side-chain conformational energy surface E = E(χ1, χ2) of N-formyl-l-serinamide (For-l-Ser-NH2) in its γL or C7eq backbone conformation

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Abstract

Since each torsional mode (χ1 about the CαCβ and χ2 about the CβO bond) of the side-chain of N-formyl-lserinamide, For-l-Ser-NH2, is expected to have three minima (g+, a, g-), {A figure is presented} the side chain conformational potential energy surface (PES) E = E(χ1, χ2) is expected to have, in the ideal case, nine legitimate minima. {A figure is presented}. Taking 30 ° intervals along χ1 and χ2 a 12 × 12 grid of points has been generated to examine the side-chain conformational PES using a rigid γL(C7eq) backbone conformation (γL; φ = -75 °, ψ = +75 °). Six out of the nine expected minima have been located on the ab initio PES generated for the γL backbone conformation, at the HF/3-21G level of theory. However, three conformations were missing. The relaxed geometries of the remaining six side-chain conformations have been determined by gradient geometry optimization.

Original languageEnglish
Pages (from-to)27-36
Number of pages10
JournalJournal of Molecular Structure: THEOCHEM
Volume331
Issue number1-2
DOIs
Publication statusPublished - Jan 20 1995

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Carbon Monoxide
Interfacial energy
Potential energy surfaces
surface energy
peptides
Conformations
Peptides
potential energy
Geometry
geometry
grids
intervals
gradients
optimization
serinamide

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Condensed Matter Physics

Cite this

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title = "Peptide models XIII. Side-chain conformational energy surface E = E(χ1, χ2) of N-formyl-l-serinamide (For-l-Ser-NH2) in its γL or C7eq backbone conformation",
abstract = "Since each torsional mode (χ1 about the CαCβ and χ2 about the CβO bond) of the side-chain of N-formyl-lserinamide, For-l-Ser-NH2, is expected to have three minima (g+, a, g-), {A figure is presented} the side chain conformational potential energy surface (PES) E = E(χ1, χ2) is expected to have, in the ideal case, nine legitimate minima. {A figure is presented}. Taking 30 ° intervals along χ1 and χ2 a 12 × 12 grid of points has been generated to examine the side-chain conformational PES using a rigid γL(C7eq) backbone conformation (γL; φ = -75 °, ψ = +75 °). Six out of the nine expected minima have been located on the ab initio PES generated for the γL backbone conformation, at the HF/3-21G level of theory. However, three conformations were missing. The relaxed geometries of the remaining six side-chain conformations have been determined by gradient geometry optimization.",
author = "O. Farkas and A. Perczel and Marcoccia, {J. F.} and M. Holl{\'o}si and I. Csizmadia",
year = "1995",
month = "1",
day = "20",
doi = "10.1016/0166-1280(94)03929-F",
language = "English",
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pages = "27--36",
journal = "Computational and Theoretical Chemistry",
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T1 - Peptide models XIII. Side-chain conformational energy surface E = E(χ1, χ2) of N-formyl-l-serinamide (For-l-Ser-NH2) in its γL or C7eq backbone conformation

AU - Farkas, O.

AU - Perczel, A.

AU - Marcoccia, J. F.

AU - Hollósi, M.

AU - Csizmadia, I.

PY - 1995/1/20

Y1 - 1995/1/20

N2 - Since each torsional mode (χ1 about the CαCβ and χ2 about the CβO bond) of the side-chain of N-formyl-lserinamide, For-l-Ser-NH2, is expected to have three minima (g+, a, g-), {A figure is presented} the side chain conformational potential energy surface (PES) E = E(χ1, χ2) is expected to have, in the ideal case, nine legitimate minima. {A figure is presented}. Taking 30 ° intervals along χ1 and χ2 a 12 × 12 grid of points has been generated to examine the side-chain conformational PES using a rigid γL(C7eq) backbone conformation (γL; φ = -75 °, ψ = +75 °). Six out of the nine expected minima have been located on the ab initio PES generated for the γL backbone conformation, at the HF/3-21G level of theory. However, three conformations were missing. The relaxed geometries of the remaining six side-chain conformations have been determined by gradient geometry optimization.

AB - Since each torsional mode (χ1 about the CαCβ and χ2 about the CβO bond) of the side-chain of N-formyl-lserinamide, For-l-Ser-NH2, is expected to have three minima (g+, a, g-), {A figure is presented} the side chain conformational potential energy surface (PES) E = E(χ1, χ2) is expected to have, in the ideal case, nine legitimate minima. {A figure is presented}. Taking 30 ° intervals along χ1 and χ2 a 12 × 12 grid of points has been generated to examine the side-chain conformational PES using a rigid γL(C7eq) backbone conformation (γL; φ = -75 °, ψ = +75 °). Six out of the nine expected minima have been located on the ab initio PES generated for the γL backbone conformation, at the HF/3-21G level of theory. However, three conformations were missing. The relaxed geometries of the remaining six side-chain conformations have been determined by gradient geometry optimization.

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