Studying the structural properties of polyalanine and polyglutamine peptides

Balázs Leitgeb, Ádám Kerényi, F. Bogár, Gábor Paragi, B. Penke, G. Rákhely

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Poly-(Ala) and poly-(Gln) peptides have important biological effects, and can cause various human illnesses and neurodegenerative diseases. Conformational analysis of these homo-oligopeptides (HOPs) was carried out by simulated annealing in order to identify their structural properties regarding secondary structures and intramolecular H-bonding patterns. Poly-(Ala) and poly-(Gln) peptides composed of 7, 10, 14 or 20 amino acids were modelled in both charged and terminally blocked forms. In the case of conformers derived from simulated annealing calculations, the presence of various secondary structural elements (different types of β-turns, α-helix, 310-helix, poly-proline II helix, parallel and antiparallel β-strands) was investigated. Moreover, the intramolecular H-bonding patterns formed either between the backbone atoms for both HOPs or between the backbone and side-chain atoms for the poly-(Gln) peptides were examined. Our results showed that different secondary structural elements (type I and type III β-turns, α-helix, 310-helix, antiparallel β-strand) could be observed in both poly-(Ala) and poly-(Gln) peptides and, according to their presence, characteristic H-bonding patterns formed mainly by i←i+3 and i←i+4 H-bonds could be found.

Original languageEnglish
Pages (from-to)1141-1150
Number of pages10
JournalJournal of Molecular Modeling
Volume13
Issue number11
DOIs
Publication statusPublished - 2007

Fingerprint

helices
Peptides
peptides
Structural properties
Oligopeptides
Simulated annealing
simulated annealing
strands
Neurodegenerative diseases
Atoms
Proline
Neurodegenerative Diseases
biological effects
Amino acids
amino acids
atoms
Amino Acids
polyglutamine
polyalanine
causes

Keywords

  • Homo-oligopeptides
  • Intramolecular H-bond
  • Polyalanine
  • Polyglutamine
  • Secondary structure

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Computer Science Applications
  • Computational Theory and Mathematics
  • Catalysis
  • Organic Chemistry
  • Inorganic Chemistry
  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics

Cite this

Studying the structural properties of polyalanine and polyglutamine peptides. / Leitgeb, Balázs; Kerényi, Ádám; Bogár, F.; Paragi, Gábor; Penke, B.; Rákhely, G.

In: Journal of Molecular Modeling, Vol. 13, No. 11, 2007, p. 1141-1150.

Research output: Contribution to journalArticle

Leitgeb, Balázs ; Kerényi, Ádám ; Bogár, F. ; Paragi, Gábor ; Penke, B. ; Rákhely, G. / Studying the structural properties of polyalanine and polyglutamine peptides. In: Journal of Molecular Modeling. 2007 ; Vol. 13, No. 11. pp. 1141-1150.
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