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用异核多维NMR技术研究蛋白质动力学 被引量:5

PROTEIN DYNAMICS STUDIED BY HETERONUCLEAR MULTI-DIMENSIONAL NMR
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摘要 蛋白质在溶液中的三维空间结构、动力学与蛋白质生物功能的关系是在分子水平上理解生命现象的重要基础 .NMR技术在研究蛋白质动力学方面具有独特的优势 ,所能表征的运动过程相关时间尺度很广 .文章综述了异核多维NMR技术研究蛋白质动力学的实验技术和理论方法 ,介绍了描述蛋白质动力学的内运动参量的意义和Model Free方法 ,并举例说明1 One of the fundamental problems in understanding life science at the molecular level is the relationship among structure, dynamics, and function of proteins. NMR has a unique capacity to investigate dynamics properties of proteins over a range of different time scales with atomic resolution. This review focuses on the experimental and theoretical methods used in heteronuclear spin relaxation measurement for studying protein dynamics, and the parameters describing the protein internal motion as well as the Model-Free method. Finally, some application examples are given in which ^(15)N relaxation measurements were performed to study the backbone dynamics of protein and protein-ligand complex.
出处 《波谱学杂志》 CAS CSCD 北大核心 2004年第4期385-396,共12页 Chinese Journal of Magnetic Resonance
基金 中国科学院"百人计划"研究基金 上海市重点基础研究基金 ( 0 3JC140 81) 厦门大学预研基金资助项目
关键词 蛋白质 配体 运动 研究 分子水平 实验 生物功能 NMR技术 动力学 弛豫 heteronuclear NMR, protein, relaxation, dynamics, mobility
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  • 1Palmer A G. NMR Probes of Molecular Dynamics: Overview and comparison with other Techniques[J]. Annu Rev Bioph Biom Struct, 2001, 30: 129-155. 被引量:1
  • 2(a) Palmer A G. Probing molecular motion by NMR[J]. Curr Opin Struc Biol, 1997, 7: 732-737; (b) Palmer A G, Kroenke C D, Loria J P. Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules[J]. Method Enzymol, 2001, 339: 204-238; (c) Fischer M W F, Majumdar A, Zuiderweg E R P. Protein NMR relaxation: theory, applications and outlook[J]. Prog Nucl Mag Res Spect, 1998, 33: 207-272. 被引量:1
  • 3(a) Hernandez G, LeMaster D M. Reduced temperature dependence of collective conformational opening in a hyperthermophile rubredoxin[J]. Biochemistry, 2001, 40: 14 384-14 391; (b) Hernandez G, Jenney F E Jr, Adams M W W, et al. Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature[J]. Proc Nat Acad Sci USA, 2000, 97: 3 166-3 170. 被引量:1
  • 4Chou J J, Case D A, Bax A. Insights into the mobility of methyl-bearing side chains in proteins from 3JCC and 3JCN couplings[J]. J Am Chem Soc, 2003, 125: 8 959-8 966. 被引量:1
  • 5(a) Tolman J R. A novel approach to the retrieval of structural and dynamic information from residual dipolar couplings using several oriented media in biomolecular NMR spectroscopy[J]. J Am Chem Soc, 2002, 124: 12 020-12 030; (b) Meiler J, Peti W, Griesinger C. Dipolar couplings in multiple alignments suggest alpha helical motion in ubiquitin[J]. J Am Chem Soc, 2003, 125: 8 072-8 073; (c) Briggman K B, Tolman J R. De novo determination of bond orientations and order parameters from residual dipolar couplings with high accuracy[J]. J Am Chem Soc, 2003, 125: 10 164-10 165; (d) Clore G M, Schwieters C D. How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation[J]. J Am Chem Soc, 2004, 126: 2 923-2 938. 被引量:1
  • 6Allerhand A, Doddrell D, Glushko V, et al. Conformation and segmental motion of native and denatured ribonuclease A in solution. Application of natural-abundance carbon-13 partially relaxed Fourier transform nuclear magnetic resonance[J]. J Am Chem Soc, 1971, 93: 544-546. 被引量:1
  • 7Gust D, Moon R B, Roberts J D. Applications of natural-abundance nitrogen-15 nuclear magnetic resonance to large biochemically important molecules[J]. Proc Nat Acad Sci USA, 1975, 72: 4 649-4 700. 被引量:1
  • 8(a) McCain D C, Markley J L. Rotational spectral density functions for aqueous sucrose: experimental determination using carbon-13 NMR[J]. J Am Chem Soc, 1986, 108: 4 259-4 264; (b) Schiksnis R A, Bogusky M J, Tsang P, et al. Structure and dynamics of the Pf1 filamentous bacteriophage coat protein in micelles[J]. Biochemistry, 1989, 28: 1 373-1 381; (c) Henry G D, Weiner J H, Sykes B D. Backbone dynamics of a model membrane protein: 3C NMR spectroscopy of alanine methyl groups in detergent-solubilized M13 coat protein[J]. Biochemistry, 1986, 25: 590-598. 被引量:1
  • 9Kay L E, Torchia D A, Bax A. Backbone dynamics of proteins as studied by 5N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease[J]. Biochemistry, 1989, 28: 8 972-8 979. 被引量:1
  • 10(a) Boyd J. Short selective pulses for biochemical applications[J]. J Magn Reson, 1995, B106(3): 300-303; (b) Buck M, Boyd J, Redfield C, et al. Structural determinants of protein dynamics: analysis of 5N NMR relaxation measurements for main-chain and side-chain nuclei of hen egg white lysozyme[J]. Biochemistry, 1995, 34: 4 041-4 055. 被引量:1

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