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)

doi:10.7523/j.issn.2095-6134.2002.2.021

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

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

Institute of Biophysics of the Chinese Academy of Sciences, Beijing 100101

Received:2002-01-29 Published:2002-03-18

摘要/Abstract

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

中图分类号:

李剑, 王志珍. 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)[J]. 中国科学院大学学报, 2002, 19(2): 215-218.

LI Jian, WANG Zhi-Zhen. Effects of Molecular Chaperone, Protein Aggregation and Macromolecular Crowding on Protein Folding[J]. , 2002, 19(2): 215-218.

参考文献

[1] Li X L, Lei X D, Cai H, Li J, Yang S L, Wang C C, T sou C L.Binding of a burst-phase intermediate formed in the folding of denatured D-glyceraldehyde-3-phosphate dehydrogenase by chaperonin 60 and 8-anilino-1-naphthalenesulphonic acid.J Biochem, 1998, 331:505～ 511

[2] Li J, Wang C-C.Half of the sites"binding of D-glyceraldehyde-3-phosphate dehydrogenase folding intermediate with G roEL.J Biol Chem, 1999, 274 :10790 ～ 10794

[3] Zhang S, Li J, Wang C C, Tsou C L.Metal regulation of metallothionein participation in redox reactions.FEBS Lett, 1999, 462:383～ 386

[4] Zhang N X, Li J, Wang C C.GroEL and protein disulfide isomerase each binds with folding intermediates of D-glyceraldehyde-3-phosphate dehydrogenase released from complexes formed wi th the ot her.J Prot ein Chem, 2000, 19 :569 ～ 574

[5] Li J, Lin Z, Wang C C.Aggregated proteins accelerate but do not increase the aggregation of D-glyceraldehyde-3-phosphate dehydrogenase———specificity of protein aggregation.J Protein Chem, 2001, 20:155～ 163

[6] Li J, Zhang S, Wang C C.Only the reduced conformerof α-lactalbumin is inducible to aggregation by protein aggregates.J Biochem(Toky-o), 2001, 129 :821 ～ 826

[7] Zhang S, Li J, Wang C C.GroEL-assisted dehydrogenase folding mediatedby coenzyme isATP-independent.Biochem Biophys Res Comm,2001, 285 :277 ～ 282

[8] Liang Y, Li J, Chen J, Wang C C.Thermodynamics of the folding of D-glyceraldehyde-3-phosphate dehydrogenase assisted by protein disul-f ide isomerase st udied by mi crocalorimetry.Eu r J Biochem, 2001, 268 :4183 ～ 4189

[9] Li J, Zhang S, Wang C C.Effects of macromolecular crowding on the refolding of glucose-6-phosphate dehydrogenase and protein disulfide isomerase.J Biol Chem, 2001, 276 :34396 ～ 34401

[10] Li J, Wang C C.细胞内的大分子拥挤环境.生物化学与生物物理进展, 2001, 28:788～ 792

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)

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

PDF (PC)

可视化

摘要/Abstract

引用本文

使用本文

参考文献

相关文章 6

编辑推荐

Metrics

本文评价

访问统计

联系我们

[1]	刘广, 李良, 赵润宁, 陈杭, 李丹, 韩聚广. MCL-1及其BH3 螺旋结合自由能计算研究蛋白-蛋白相互作用原理[J]. 中国科学院大学学报, 2012, 29(5): 605-613.
[2]	牛建楼, 刘白玲, 王斌. 促蛋白复性高分子及其作用机制[J]. 中国科学院大学学报, 2012, 29(5): 693-698.
[3]	王喆, 张洁, 赵宇亮, 秘晓林. 肿瘤抑制因子Caliban相互作用蛋白的筛选和验证[J]. 中国科学院大学学报, 2011, 28(4): 481-488.
[4]	彭钢, 刘白玲, 赵春霞, 江正武. 导数紫外光谱法研究pH诱导牛血清蛋白构象变化[J]. 中国科学院大学学报, 2011, 28(1): 12-18.
[5]	李敏康钱冬明宋宏新. 猪血浆中凝血酶、免疫球蛋白等功能蛋白的联合提取[J]. 中国科学院大学学报, 2007, 24(3): 357-361.
[6]	刘安源, 刘石, 潘忠刚. 振动给料机中固体颗粒物料运动规律的数值研究[J]. 中国科学院大学学报, 2002, 19(1): 35-42.