ArticleJournal of molecular modeling2007
Studying the structural properties of polyalanine and polyglutamine peptides.
Article in Journal of molecular modeling, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Tandem repeats in human brain evolution and disease susceptibility.Molecules and cells · 2026Review
- Bioinformatic Analyses of the Ataxin-2 Family Since Algae Emphasize Its Small Isoforms, Large Chimerisms, and the Importance of Human Exon 1B as Target of Therapies to Prevent Neurodegeneration.International journal of molecular sciences · 2026Article
- Impact of a conserved N-terminal proline-rich region of the α-subunit of CAAX-prenyltransferases on their enzyme properties.Cell communication and signaling : CCS · 2022Article
- Amino acid homorepeats in proteins.Nature reviews. Chemistry · 2020Review
- Intrinsic Disorder in Proteins with Pathogenic Repeat Expansions.Molecules (Basel, Switzerland) · 2017Review
- Review
- Conformational behavior of polyalanine peptides with and without protecting groups of varying chain lengths: population of PP-II structure!Journal of molecular modeling · 2015Article
- In silico conformational analysis of the short-sequence hypomurocin a peptides.International journal of peptides · 2015Article
- Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.Journal of molecular biology · 2012Review
- Essential role of coiled coils for aggregation and activity of Q/N-rich prions and PolyQ proteins.Cell · 2010Article
- N-terminal inactivation domains of beta subunits are protected from trypsin digestion by binding within the antechamber of BK channels.The Journal of general physiology · 2009Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
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 beta-turns, alpha-helix, 3(10)-helix, poly-proline II helix, parallel and antiparallel beta-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 beta-turns, alpha-helix, 3(10)-helix, antiparallel beta-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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Registered trials
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