Helix compactness and stability: Electron structure calculations of conformer dependent thermodynamic functions

Imre Jákli, Imre G. Csizmadia, Szilard N. Fejer, Ödön Farkas, Bela Viskolcz, Svend J. Knak Jensen, Andras Perczel

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Structure, stability, cooperativity and molecular packing of two major backbone forms: 310-helix and β-strand are investigated. Long models HCO-(Xxx)n-NH2 Xxx = Gly and (l-)Ala, n ≤ 34, are studied at two levels of theory including the effect of dispersion forces. Structure and folding preferences are established, the length modulated cooperativity and side-chain determined fold compactness is quantified. By monitoring ΔG°β→α rather than the electronic energy, ΔEβ→α, it appears that Ala is a much better helix forming residue than Gly. The achiral Gly forms a more compact 310-helix than any chiral amino acid residue probed here for l-Ala.

Original languageEnglish
Pages (from-to)80-87
Number of pages8
JournalChemical Physics Letters
Volume563
DOIs
Publication statusPublished - Mar 20 2013

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

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