An ab initio exploratory study on selected conformational features of MeCO-L-Ala-L-Ala-L-Ala-NH-Me as a XxxYyyZzz tripeptide motif within a protein structure

Michelle A. Sahai, Michael R. Sahai, Gregory A. Chass, Botond Penke, Imre G. Csizmadia

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

A conformational study of the tripeptide model MeCO-L-Ala-L-Ala-L-Ala-NH- Me was carried out using ab initio molecular orbital computations in order to investigate the preferred conformations. At any particular instant, two alanine residues were fixed at the [βL] conformation and the third was varied for the nine possible minima present on the Ramachandran map. Subsequently, all minima were optimized. The conformational and energetic consequences of these findings are discussed in terms of relative stabilities and degree of backbone twisting or foldedness.

Original languageEnglish
Pages (from-to)327-336
Number of pages10
JournalJournal of Molecular Structure: THEOCHEM
Volume666-667
DOIs
Publication statusPublished - Dec 29 2003

Keywords

  • Ab initio
  • Alanine motifs
  • Alanine residue
  • MeCO-L-Ala-L-Ala-L-Ala-NH-Me
  • Molecular orbital computations
  • Tripeptide

ASJC Scopus subject areas

  • Biochemistry
  • Condensed Matter Physics
  • Physical and Theoretical Chemistry

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