物理化学学报 >> 2001, Vol. 17 >> Issue (07): 619-621.doi: 10.3866/PKU.WHXB20010709

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β-转角肽的溶液构象

高峰;沙印林;邱阳;王跃丰;李银玲;来鲁华;吴厚铭   

  1. 北京大学物理化学研究所，化学与分子工程学院　分子动态与稳态国家重点实验室,北京 100871;北京大学基础医学院，生物物理系,北京 100083;中国科学院上海有机化学研究所,上 海　200032
  • 收稿日期:2001-02-12 修回日期:2001-03-15 发布日期:2001-07-15
  • 通讯作者:

Solution Conformation Study on a β-turn Forming Peptide

Gao Feng;Sha Yin-Lin;Qiu Yang;Wang Yue-Feng;Li Yin-Ling;Lai Lu-Hua;Wu Hou-Ming   

  1. Institute of Physical Chemistry,College of Chemistry and Molecular Engineering ,State Key Laboratory for Structural Chemistry of Unstable ＆ Stable Species,Pek ing University,Beijing　100871;Department of Biophysics,The School of Basic Medical Sciences,Peking University,Beijing　100083;Institute of Organic Chemis try,Chinese Academy of Sciences,Shanghai　200032
  • Received:2001-02-12 Revised:2001-03-15 Published:2001-07-15
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摘要： 主要报导TEM-1β-内酰胺酶的天然蛋白类抑制剂BLIP中一段多肽B1的溶液构象研究 结果.在磷酸盐缓冲溶液中，通过圆二色光谱、傅立叶红外光谱和核磁共振谱研究了B1的二 级结构特征.实验结果表明，B1在溶液中形成了β-转角结构，为在溶液中单独研究β-转 角结构形成与稳定性提供了良好的模板.β-转角在溶液中可以独立存在，表明β-转角在 蛋白质折叠过程中可能具有重要作用.

关键词: β-转角结构, 圆二色光谱, 傅立叶红外光谱, 核磁共振光谱, 多肽

Abstract: The model six-residue linear peptide AAGDYY-NH2 from TEM-1 β-lact amase inhibitor protein and BLIP was predicted to adopt a β-turn conformation and synthesized in order to elucidate the mechanism of β-turn formation and s tability.Its structural preferences in solution were comprehensively characteriz ed using CD (circular dichroism),FT-IR and 1H-NMR spectroscopy.The set of obse rved short- and medium-range NOEs,the restrained molecular dynamics simulation ,CD and FT-IR spectroscopy were consistent with the formation of β-turn in so lution by the model peptide.The results implicate β-turn playing an important role in the process of protein folding.

Key words: β-turn, CD, FT-IR, NMR, Peptide