Studying the structural properties of polyalanine and polyglutamine peptides
Studying the structural properties of polyalanine and polyglutamine peptides
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DOI：
10.1007/s00894-007-0241-4
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发表时间：
2007-11-01
影响因子：
2.2
通讯作者：
Rakhely, Gabor
中科院分区：
文献类型：
--
作者：
Leitgeb, Balazs;Kerenyi, Adam;Rakhely, Gabor
聚（Ala）和聚（Gln）多肽具有重要的生物学效应，可引起多种人类疾病和神经退行性疾病。通过模拟退火对这些同源寡肽（HOPs）进行了构象分析，以确定其二级结构和分子内氢键模式的结构性质。由7、10、14或20个氨基酸组成的聚（Ala）和聚（Gln）肽以带电和终端阻断的形式建模。在模拟退火计算得出的构象中，研究了各种二级结构元素（不同类型的β -旋、α -螺旋、3(10)-螺旋、聚脯氨酸II螺旋、平行和反平行β -链）的存在。此外，研究了两种啤酒花的主链原子之间或聚谷氨酰胺肽的主链和侧链原子之间形成的分子内氢键模式。结果表明，在聚（Ala）和聚（Gln）肽中都可以观察到不同的二级结构元素（I型和III型β -旋、α -螺旋、3(10)-螺旋、反平行β -链），并且根据它们的存在，特征的氢键模式主要由I形成
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