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博导名单【正、副高职称】
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金长文
邮  箱: changwen(AT)pku.edu.cn
职  称:
教授
办公室地址: 北京市海淀区颐和园路5号,其他,100871
实验室地址: 北京市海淀区颐和园路5号,其他,100871
实验室主页: http://bnmrc.pku.edu.cn/JinLab.html
个人简历
教育经历
1996 - 2000 , 博士后 , 结构生物学 , 美国伊利诺伊大学
1992 - 1994 , 博士后 , 化学 , 北京大学
1990 - 1992 , 理学博士 , 物理 , 北京大学
1987 - 1990 , 理学硕士 , 物理 , 吉林大学
1983 - 1987 , 理学学士 , 物理 , 吉林大学
工作经历
2001 - 至今 , 首席科学家 , 北京核磁共振中心
2001 - 至今 , 教授 , 北京大学生命科学学院
2001 - 至今 , 教授 , 北京大学化学与分子工程学院
荣誉奖励
中国波谱学会“王天眷波谱学奖” , 2008
国家杰出青年科学基金 , 2003
教育部“长江学者奖励计划”特聘教授 , 2001
学术任职
中国波谱学会专业委员会副主任
杂志任职
《波谱学杂志》副主编
《分析测试学报》编委
科研领域描述
主要研究方向: 结构生物学,生物大分子动力学的核磁共振研究,生物核磁共振方法学。

Our research mainly focuses on studies of the structures, dynamics and biological functions of proteins, especially enzymes. In particular, we are interested in the correlation between protein dynamics (structural fluctuations over time) and their functional mechanisms. We employ Nuclear Magnetic Resonance (NMR) technique to determine the solution structures and probe the dynamic properties of bio-macromolecules. We also use biochemical methods to characterize the activity and functions of proteins both in vitro and in vivo. Our main goal is to elucidate the structural and dynamic basis of protein functions.

Protein structures and dynamics
To provide structural basis for their biological functions, we use NMR technique to determine the solution structures of proteins and protein complexes. However, protein functions essentially depend on their motions, and static structures alone cannot fully explain their functions. NMR is a powerful tool to probe the motional properties of proteins. Therefore, we use relaxation phenomena, as well as newly developed NMR methods such as PRE and RDC to investigate protein dynamics and their correlation to functions.

Protein interactions
Protein functions through interactions with other molecules (proteins, ligands, or nucleic acids). We use NMR methods to characterize protein interactions. In particular, we are interested in studying (1) interactions between enzymes and substrates during catalysis, (2) interactions between receptors and ligands in signal transduction pathways, (3) protein-protein interactions in the regulation of proteasome.

Membrane proteins
Membrane proteins play essential roles in cells. Recent advances in biochemical and NMR techniques have made it possible to use solution NMR method to study the structures and dynamics of membrane proteins. We are interested in studying the structures of protein cross-membrane translocation machineries, and to elucidate the molecular mechanism or the translocation processes.

Lab Homepage: http://bnmrc.pku.edu.cn/JinLab.html
代表性论文
1. Guan L, He P, Yang F, Zhang Y, Hu Y, Ding J, Hua Y, Zhang Y, Ye Q, Hu J, Wang T*, Jin C*, Kong D*. (2017) Sap1 is a replication initiation factor essential for the assembly of pre-replicative complex in the fission yeast Schizosaccharomyces pombe. J Biol Chem. doi: 10.1074/jbc.M116.767806. (in press)

2. Ding J, Yang C, Niu X, Hu Y*, Jin C*. (2015) HdeB chaperone activity is coupled to its intrinsic dynamic properties. Sci. Rep. 5, 16856.

3. Hu C, Yu C, Liu Y, Hou X, Liu X, Hu Y*, Jin C*. (2015) A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction. J. Biol. Chem. 290, 22262-73.

4. Hu Y, Wu Y, Li Q, Zhang W, Jin C*. (2015) Solution Structure of Yeast Rpn9: Insights for Proteasome Lid Assembly. J. Biol. Chem. 290, 6878-89.

5. Ye Q, Hu Y*, Jin C*. (2014) Conformational Dynamics of Escherichia coli Flavodoxins in Apo- and Holo-States by Solution NMR Spectroscopy. PLoS One. 9, e103936

6. Zhang Y, Hu Y*, Li H, Jin C*. (2014) Structural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric Structure. PLoS One. 9, e103157.

7. Zhang Y, Wang L, Hu Y*, Jin C*. (2014) Solution structure of the TatB component of the twin-arginine translocation system. Biochim. Biophys. Acta. 1838: 1881-8.

8. Liu T, Liu , Song C, Hu Y, Han Z, She J, Fan F, Wang J, Jin C, Chang J, Zhou J-M, Chai J*. (2012) Chitin-induced dimerization activates a plant immune receptor. Science 336, 1160-4.

9. Hu Y, Zhang X, Shi Y, Zhou Y, Zhang W, Su X-D, Xia B, Zhao J*, Jin C*. (2011) Structures of Anabaena calcium-binding protein CcbP: insights into Ca2+ signaling during heterocyst differentiation. J. Biol. Chem. 286, 12381-8.

10. Hu Y, Zhao E, Li H, Xia B, Jin C*. (2010) Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis. J. Am. Chem. Soc. 132, 15942-4.

11. Lescop E, Lu Z, Liu Q, Xu H, Li G, Xia B, Yan H*, Jin C*. (2009) Dynamics of the conformational transitions in the assembling of the Michaelis complex of a bisubstrate enzyme: a 15N relaxation study of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase. Biochemistry 48, 302-12.

12. Li Y, Hu Y, Zhang X, Xu H, Lescop E, Xia B, Jin C*. (2007) Conformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilis. J. Biol. Chem. 282, 11078-83.
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