Information accumulation in helical oligopeptide structures

B. Viskolcz, Szilard N. Fejer, Svend J. Knak Jensen, A. Perczel, I. Csizmadia

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

If structural information is viewed in terms of entropy of the molecule, the folded and misfolded structures of a wild-type protein and its mutant contain different amounts of information. Here we present the strong side chain-dependence of the internal entropy of folding, and consequently of the relative information content for the simplest oligopeptides. It is found that during a conformational change from extended to 310-helical structure, the (Gly)10 oligomer accumulates 106 more information than the (Ala)10 oligomer. It is argued that the difference in information accumulation is related to chirality. The role of Ala → Gly point mutation is also examined.

Original languageEnglish
Pages (from-to)123-126
Number of pages4
JournalChemical Physics Letters
Volume450
Issue number1-3
DOIs
Publication statusPublished - Dec 14 2007

Fingerprint

Oligopeptides
Oligomers
Entropy
Chirality
Mutant Proteins
oligomers
Molecules
entropy
mutations
chirality
folding
proteins
molecules
decaglycine

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Spectroscopy
  • Atomic and Molecular Physics, and Optics
  • Surfaces and Interfaces
  • Condensed Matter Physics

Cite this

Information accumulation in helical oligopeptide structures. / Viskolcz, B.; Fejer, Szilard N.; Knak Jensen, Svend J.; Perczel, A.; Csizmadia, I.

In: Chemical Physics Letters, Vol. 450, No. 1-3, 14.12.2007, p. 123-126.

Research output: Contribution to journalArticle

Viskolcz, B. ; Fejer, Szilard N. ; Knak Jensen, Svend J. ; Perczel, A. ; Csizmadia, I. / Information accumulation in helical oligopeptide structures. In: Chemical Physics Letters. 2007 ; Vol. 450, No. 1-3. pp. 123-126.
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