Information accumulation in helical oligopeptide structures

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

Research output: Contribution to journalArticle

6 Citations (Scopus)


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
Issue number1-3
Publication statusPublished - Dec 14 2007

ASJC Scopus subject areas

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

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