Peptide models VII The ending of the right-handed helices in oligopeptides [For-(Ala)n-NH2 for 2 ≤ n ≤ 4] and in proteins

András Perczel, Gábor Endrédi, Michael A. McAllister, Ödön Farkas, Pál Császár, János Ladik, Imre G. Csizmadia

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19 Citations (Scopus)

Abstract

The right-handed helical conformation (denoted as αL) of a single amino-acid diamide (e.g. HCONHCHCH3CO NH2) is not a minimum energy conformation on the ab initio potential energy surface. Computations performed on oligopeptides [For-(Ala)n NH2, for n ≤ 4], revealed that the helix-like conformations do exist if the backbone conformation at the carboxyl-end is of δL type; i.e. (αL)n - 1δL. This suggests that according to SCF computations, the isolated helices end in a type I β-turn (αLδL).

Original languageEnglish
Pages (from-to)5-10
Number of pages6
JournalJournal of Molecular Structure: THEOCHEM
Volume331
Issue number1-2
DOIs
Publication statusPublished - Jan 20 1995

ASJC Scopus subject areas

  • Biochemistry
  • Condensed Matter Physics
  • Physical and Theoretical Chemistry

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