NMR-Based Methods for Protein Analysis

被引:70
作者
Hu, Yunfei [1 ,2 ]
Cheng, Kai [1 ]
He, Lichun [1 ,2 ]
Zhang, Xu [1 ,2 ]
Jiang, Bin [1 ,2 ]
Jiang, Ling [1 ,2 ]
Li, Conggang [1 ,2 ]
Wang, Guan [1 ,2 ]
Yang, Yunhuang [1 ,2 ]
Liu, Maili [1 ,2 ]
机构
[1] Huazhong Univ Sci & Technol, Wuhan Inst Phys & Math,State Key Lab Magnet Reson, Innovat Acad Precis Measurement Sci & Technol,Key, Natl Ctr Magnet Resonance Wuhan,Chinese Acad Sci, Wuhan 430071, Peoples R China
[2] Univ Chinese Acad Sci, Beijing 10049, Peoples R China
关键词
D O I
10.1021/acs.analchem.0c03830
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
Nuclear magnetic resonance (NMR) spectroscopy is a well-established method for analyzing protein structure, interaction, and dynamics at atomic resolution and in various sample states including solution state, solid state, and membranous environment. Thanks to rapid NMR methodology development, the past decade has witnessed a growing number of protein NMR studies in complex systems ranging from membrane mimetics to living cells, which pushes the research frontier further toward physiological environments and offers unique insights in elucidating protein functional mechanisms. In particular, in-cell NMR has become a method of choice for bridging the huge gap between structural biology and cell biology. Herein, we review the recent developments and applications of NMR methods for protein analysis in close-to-physiological environments, with special emphasis on in-cell protein structural determination and the analysis of protein dynamics, both difficult to be accessed by traditional methods.
引用
收藏
页码:1866 / 1879
页数:14
相关论文
共 188 条
  • [1] Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus
    Acharya, Rudresh
    Carnevale, Vincenzo
    Fiorin, Giacomo
    Levine, Benjamin G.
    Polishchuk, Alexei L.
    Balannik, Victoria
    Samish, Ilan
    Lamb, Robert A.
    Pinto, Lawrence H.
    DeGrado, William F.
    Klein, Michael L.
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2010, 107 (34) : 15075 - 15080
  • [2] Large cosolutes, small cosolutes, and dihydrofolate reductase activity
    Acosta, Luis C.
    Goncalves, Gerardo M. Perez
    Pielak, Gary J.
    Gorensek-Benitez, Annelise H.
    [J]. PROTEIN SCIENCE, 2017, 26 (12) : 2417 - 2425
  • [3] PREPARATION OF PROTEIN SAMPLES FOR NMR STRUCTURE, FUNCTION, AND SMALL-MOLECULE SCREENING STUDIES
    Acton, Thomas B.
    Xiao, Rong
    Anderson, Stephen
    Aramini, James
    Buchwald, William A.
    Ciccosanti, Colleen
    Conover, Ken
    Everett, John
    Hamilton, Keith
    Huang, Yuanpeng Janet
    Janjua, Haleema
    Kornhaber, Gregory
    Lau, Jessica
    Lee, Dong Yup
    Liu, Gaohua
    Maglaqui, Melissa
    Ma, Lichung
    Mao, Lei
    Patel, Dayaban
    Rossi, Paolo
    Sahdev, Seema
    Shastry, Ritu
    Swapna, G. V. T.
    Tang, Yeufeng
    Tong, Saichiu
    Wang, Dongyan
    Wang, Huang
    Zhao, Li
    Montelione, Gaetano T.
    [J]. FRAGMENT-BASED DRUG DESIGN: TOOLS, PRACTICAL APPROACHES, AND EXAMPLES, 2011, 493 : 21 - 60
  • [4] A Unified Description of Intrinsically Disordered Protein Dynamics under Physiological Conditions Using NMR Spectroscopy
    Adamski, Wiktor
    Salvi, Nicola
    Maurin, Damien
    Magnat, Justine
    Milles, Sigrid
    Jensen, Malene Ringkjobing
    Abyzov, Anton
    Moreau, Christophe J.
    Blackledge, Martin
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2019, 141 (44) : 17817 - 17829
  • [5] Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy
    Amata, Irene
    Maffei, Mariano
    Igea, Ana
    Gay, Marina
    Vilaseca, Marta
    Nebreda, Angel R.
    Pons, Miquel
    [J]. CHEMBIOCHEM, 2013, 14 (14) : 1820 - 1827
  • [6] Structure and Mechanism of the Influenza A M218-60 Dimer of Dimers
    Andreas, Loren B.
    Reese, Marcel
    Eddy, Matthew T.
    Gelev, Vladimir
    Ni, Qing Zhe
    Miller, Eric A.
    Emsley, Lyndon
    Pintacuda, Guido
    Chou, James J.
    Griffin, Robert G.
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2015, 137 (47) : 14877 - 14886
  • [7] In Situ Cryo-Electron Tomography: A Post-Reductionist Approach to Structural Biology
    Asano, Shoh
    Engel, Benjamin D.
    Baumeister, Wolfgang
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2016, 428 (02) : 332 - 343
  • [8] Validation of protein structure from preparations of encapsulated proteins dissolved in low viscosity fluids
    Babu, CR
    Flynn, PF
    Wand, AJ
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2001, 123 (11) : 2691 - 2692
  • [9] Macromolecular and Small Molecular Crowding Have Similar Effects on α-Synuclein Structure
    Bai, Jia
    Liu, Maili
    Pielak, Gary J.
    Li, Conggang
    [J]. CHEMPHYSCHEM, 2017, 18 (01) : 55 - 58
  • [10] Banci L, 2013, NAT CHEM BIOL, V9, P297, DOI [10.1038/NCHEMBIO.1202, 10.1038/nchembio.1202]