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Neighbor Effect on PPII Conformation in Alanine Peptides

机译:邻域对丙氨酸肽中PPII构象的影响

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摘要

Unfolded polypeptides have been demonstrated to have significant local structure while obeying overall random coil chain statistics.In particular the backbone polyproline II (PPII) (O = -75°,PSI = +145°) conformation is present in unfolded proteins and short peptides7 as well as coil libraries from the PDB.Temperature studies show that PPII conformation is in equilibrium with beta structure.
机译:已证明未折叠的多肽具有显着的局部结构,同时遵循总体随机螺旋链统计数据,尤其是未折叠的蛋白质和短肽中存在骨架多脯氨酸II(PPII)(O = -75°,PSI = + 145°)构象。温度研究表明PPII构象与β结构处于平衡状态。

著录项

  • 来源
    《Journal of the American Chemical Society》 |2005年第29期|p.10146-10147|共2页
  • 作者单位

    Department of Chemistry,New York University,100 Washington Square East,New York,New York 10003;

    Department of Chemistry,New York University,100 Washington Square East,New York,New York 10003;

    Department of Chemistry,New York University,100 Washington Square East,New York,New York 10003;

    Department of Chemistry,New York University,100 Washington Square East,New York,New York 10003;

    Department of Chemistry,New York University,100 Washington Square East,New York,New York 10003;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 化学;
  • 关键词

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