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蛋白质溶液结构及动力学的核磁共振研究 被引量:8

NMR Studies of Protein Solution Structures and Dynamics
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摘要 高场液相核磁共振技术作为解析高分辨率蛋白质结构的两大主要手段之一,在近二十几年的时间里得到了迅猛的发展.一方面,随着谱仪硬件技术、核磁脉冲技术和蛋白质标记技术的不断发展,液相核磁共振技术所能够研究的蛋白质不断突破分子量的限制,可以达到几万,甚至几十万.另一方面,液相核磁共振技术成功地应用于蛋白质分子动力学的研究中,是目前唯一能够对蛋白质多个位点同时进行动力学研究的实验方法,并且仍在不断地创新、发展和完善中.本文从蛋白质溶液结构的解析和动力学的研究两个主要方面对液相核磁共振研究的基本方法进行简要的介绍,并结合实例介绍一些最新的研究进展. As one of the major techniques for determining high-resolution protein structures, high-field solution NMR has achieved remarkable developments during the past twenty years. With the advances of advanced spectrometer hardware, NMR pulse techniques and protein labeling strategies, the size of the protein that can be studied by solution NMR now exceeds 25 k, and can reach tens and even hundreds of kilo Dalton. In addition, solution NMR has also been widely used in the studies of protein dynamics, and is the only technology that can be used to probe protein motions at multiple sites simultaneously. In this review, we briefly summarize the methods for studying protein structures and dynamics using solution NMR, accompanied by examples to demonstrate the latest developments in the field.
出处 《波谱学杂志》 CAS CSCD 北大核心 2009年第2期151-172,共22页 Chinese Journal of Magnetic Resonance
基金 国家杰出青年科学基金资助项目(30325010)
关键词 核磁共振(NMR) 蛋白质结构 动力学 NMR, protein structure, dynamics
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  • 1Wuthrich K. NMR of Proteins and Nucleic Acids[M]. New York: Wiley-Interscience, 1986.
  • 2Hibler D W, Harpold L, Dell'Acqua M, et al. Isotopic labeling with hydrogen-2 and carbon-13 to compare conformations of proteins and mutants generated by site-directed mutagenesis, I[J].Methods Enzymol, 1989, 177: 74-86.
  • 3Muchmore D C, Mclntosh L P, Russell C 13, et al. Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance[J]. Methods Enzymol, 1989, 177: 44-73.
  • 4Goto N K, Kay L E. New developments in isotope labeling strategies for protein solution NMR spectroscopy[J]. Curt Opin Struct Biol, 2000, 10(5) : 585-592.
  • 5Ohki S-y, Kainosho M. Stable isotope labeling methods for protein NMR spectroscopy[J].Prog Nucl Magn Reson Spectrosc, 2008, 53(4): 208-226.
  • 6Kay L E. Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution[J]. Prog Biophys Mol Biol, 1995, 63(3): 277-299.
  • 7Sattler M, Schleucher J, Griesinger C. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients[J]. Prog Nucl Magn Reson Spectrosc, 1999, 34(2): 93-158.
  • 8Ikura M, Kay L E, Bax A. A novel approach for sequential assignment of ^1H, ^13C, and ^15N spectra of larger proteins: Heteronuelear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin[J]. Biochemistry, 1990, 29(19): 4 659-4 667.
  • 9Kay L E, Ikura M, Tschudin R, et al. Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins[J].J Magn Reson, 1990, 89(3): 496-514.
  • 10Powers R, Gronenborn A M, Clore G M, et al. Three-dimensional triple-resonance NMR of ^13C/^15N-enriched proteins using constant-time evolution[J]. J Magn Reson, 1991, 94(1): 209-213.

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