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

Research output: Contribution to journalArticle

52 Citations (Scopus)

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

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Fingerprint Dive into the research topics of 'Peptide models. 18. Hydroxymethyl side-chain induced backbone conformational shifts of L-serine amide. All ab initio conformers of For-L-Ser-NH<sub>2</sub>'. Together they form a unique fingerprint.

  • Cite this