Peptide models. 18. Hydroxymethyl side-chain induced backbone conformational shifts of L-serine amide. All ab initio conformers of For-L-Ser-NH2

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Abstract

Using ab initio conformational energy mapping (HF/3-21G) a maximum of nine characteristic backbone conformation clusters (αL, αD, βL, γL, γD, δL, δD, εL, and εD) were previously established for different amino acid diamides (e.g., For-L-Ala-NH2, For-L-Val-NH2, and For-L-Phe-NH2). Most of the above nine backbone conformers have been located in thc [φ,ψ] space for various side-chain conformers. The present conformation analysis derives structural parameters of For-L-Ser-NH2 molecule based on a systematic investigation of the side-chain conformational energy maps {E = E(χ12)} associated with characteristic backbone structures. The systematic mapping of the E = E(φ,ψ,χ12) four-dimensional Ramachandran-type map has revealed 44 minima. This finding thus established the complete conformational set for For-L-Ser-NH2. Specific intramolecular hydrogen bonds of the 44 geometry optimized structures were analyzed. These ab initio structures can now be used with greater confidence during force field parameterizations, NMR, and X-ray structure elucidations or even for the characterization of protein backbone structures.

Original languageEnglish
Pages (from-to)7809-7817
Number of pages9
JournalJournal of the American Chemical Society
Volume118
Issue number33
DOIs
Publication statusPublished - Aug 21 1996

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Amides
Serine
Peptides
Conformations
Diamide
Parameterization
Structural analysis
Amino acids
Hydrogen
Hydrogen bonds
Nuclear magnetic resonance
X-Rays
Proteins
Amino Acids
X rays
Molecules
Geometry
serinamide

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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title = "Peptide models. 18. Hydroxymethyl side-chain induced backbone conformational shifts of L-serine amide. All ab initio conformers of For-L-Ser-NH2",
abstract = "Using ab initio conformational energy mapping (HF/3-21G) a maximum of nine characteristic backbone conformation clusters (αL, αD, βL, γL, γD, δL, δD, εL, and εD) were previously established for different amino acid diamides (e.g., For-L-Ala-NH2, For-L-Val-NH2, and For-L-Phe-NH2). Most of the above nine backbone conformers have been located in thc [φ,ψ] space for various side-chain conformers. The present conformation analysis derives structural parameters of For-L-Ser-NH2 molecule based on a systematic investigation of the side-chain conformational energy maps {E = E(χ1,χ2)} associated with characteristic backbone structures. The systematic mapping of the E = E(φ,ψ,χ1,χ2) four-dimensional Ramachandran-type map has revealed 44 minima. This finding thus established the complete conformational set for For-L-Ser-NH2. Specific intramolecular hydrogen bonds of the 44 geometry optimized structures were analyzed. These ab initio structures can now be used with greater confidence during force field parameterizations, NMR, and X-ray structure elucidations or even for the characterization of protein backbone structures.",
author = "A. Perczel and O. Farkas and I. Csizmadia",
year = "1996",
month = "8",
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T1 - Peptide models. 18. Hydroxymethyl side-chain induced backbone conformational shifts of L-serine amide. All ab initio conformers of For-L-Ser-NH2

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AU - Farkas, O.

AU - Csizmadia, I.

PY - 1996/8/21

Y1 - 1996/8/21

N2 - Using ab initio conformational energy mapping (HF/3-21G) a maximum of nine characteristic backbone conformation clusters (αL, αD, βL, γL, γD, δL, δD, εL, and εD) were previously established for different amino acid diamides (e.g., For-L-Ala-NH2, For-L-Val-NH2, and For-L-Phe-NH2). Most of the above nine backbone conformers have been located in thc [φ,ψ] space for various side-chain conformers. The present conformation analysis derives structural parameters of For-L-Ser-NH2 molecule based on a systematic investigation of the side-chain conformational energy maps {E = E(χ1,χ2)} associated with characteristic backbone structures. The systematic mapping of the E = E(φ,ψ,χ1,χ2) four-dimensional Ramachandran-type map has revealed 44 minima. This finding thus established the complete conformational set for For-L-Ser-NH2. Specific intramolecular hydrogen bonds of the 44 geometry optimized structures were analyzed. These ab initio structures can now be used with greater confidence during force field parameterizations, NMR, and X-ray structure elucidations or even for the characterization of protein backbone structures.

AB - Using ab initio conformational energy mapping (HF/3-21G) a maximum of nine characteristic backbone conformation clusters (αL, αD, βL, γL, γD, δL, δD, εL, and εD) were previously established for different amino acid diamides (e.g., For-L-Ala-NH2, For-L-Val-NH2, and For-L-Phe-NH2). Most of the above nine backbone conformers have been located in thc [φ,ψ] space for various side-chain conformers. The present conformation analysis derives structural parameters of For-L-Ser-NH2 molecule based on a systematic investigation of the side-chain conformational energy maps {E = E(χ1,χ2)} associated with characteristic backbone structures. The systematic mapping of the E = E(φ,ψ,χ1,χ2) four-dimensional Ramachandran-type map has revealed 44 minima. This finding thus established the complete conformational set for For-L-Ser-NH2. Specific intramolecular hydrogen bonds of the 44 geometry optimized structures were analyzed. These ab initio structures can now be used with greater confidence during force field parameterizations, NMR, and X-ray structure elucidations or even for the characterization of protein backbone structures.

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