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中国科学院大学学报 ›› 2002, Vol. 19 ›› Issue (2): 215-218.DOI: 10.7523/j.issn.2095-6134.2002.2.021

• 博士生优秀学位论文摘登 • 上一篇    下一篇

分子伴侣、蛋白质聚集和大分子拥挤环境对蛋白质折叠的影响(英)

李剑, 王志珍   

  1. 中国科学院生物物理研究所, 北京 100101
  • 收稿日期:2002-01-29 发布日期:2002-03-18
  • 作者简介:LI Jian,male,born in February 1975,Postdoctor
  • 基金资助:

    supportedbyPandengProjectoftheChineseMinistryofScienecandTechnology;973 project(G19990 75 60 8)

Effects of Molecular Chaperone, Protein Aggregation and Macromolecular Crowding on Protein Folding

LI Jian, WANG Zhi-Zhen   

  1. Institute of Biophysics of the Chinese Academy of Sciences, Beijing 100101
  • Received:2002-01-29 Published:2002-03-18

摘要:

研究了细胞内存在的分子伴侣、蛋白质聚集和大分子拥挤环境对蛋白质折叠的影响.首先,发现分子伴侣GroEL与底物蛋白的结合有 半位 "和 全位"两种模式,它是由底物蛋白的分子形状、分子大小以及与GroEL的相互作用性质决定的.接着,发现两种不同的蛋白质一起复性时相互不干扰,提示细胞内蛋白质折叠可能不受其他蛋白聚集的影响;后又发现α 乳清蛋白的前熔球态不仅是分子伴侣也是蛋白质聚集体的作用对象.最后,研究大分子拥挤环境对蛋白质折叠热力学和动力学的影响,揭示了这种影响的复杂性和多样性.

关键词: 蛋白质折叠, 分子伴侣, 蛋白质聚集, 大分子拥挤

Abstract:

The effects of molecular chaperones, protein aggregation and macromolecular crowding on protein folding have been studied. It has been demonstrated that there are two binding ways between molecular chaperone GroEL and its substrates, "all of sites" and "half of sites", depending on the shape, the size of substrates and the interaction between GroEL and substrates. It has also provided insights into a mechanism of cells to prevent protein folding against interference from aggregation of other proteins. In addition, it has been suggested that pre-molten globule state of α-lactalbumin is the target not only for chaperones but also for protein aggregates. Finally, it has displayed the complexity and the diversity of effects of macromolecular crowding on both the thermodynamics and kinetics of protein folding and assembly.

Key words: protein folding, molecular chaperone, protein aggregation, macromolecular crowding

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