Studying the structural properties of polyalanine and polyglutamine peptides |
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Authors: | Balázs Leitgeb Ádám Kerényi Ferenc Bogár Gábor Paragi Botond Penke Gábor Rákhely |
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Institution: | (1) Institute of Biophysics, Biological Research Center of the Hungarian Academy of Sciences, Temesvári krt. 62, 6726 Szeged, Hungary;(2) Supramolecular and Nanostructured Materials Research Group of the Hungarian Academy of Sciences, University of Szeged, Dóm tér 8, 6720 Szeged, Hungary;(3) Department of Medical Chemistry, University of Szeged, Dóm tér 8, 6720 Szeged, Hungary;(4) Department of Biotechnology, University of Szeged, Temesvári krt. 62, 6726 Szeged, Hungary |
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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. |
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Keywords: | Homo-oligopeptides Polyalanine Polyglutamine Secondary structure Intramolecular H-bond |
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