Current approaches for integrating solution NMR spectroscopy and small-angle scattering to study the structure and dynamics of biomolecular complexes

被引:16
作者
Delhommel, Florent [1 ,2 ,3 ]
Gabel, Frank [4 ]
Sattler, Michael [1 ,2 ,3 ]
机构
[1] Helmholtz Zentrum Munchen, Inst Struct Biol, Ingolstadter Landstr 1, D-85764 Neuherberg, Germany
[2] Tech Univ Munich, Bavarian NMR Ctr, Garching, Germany
[3] Tech Univ Munich, Ctr Integrated Prot Sci Munich, Dept Chem, Garching, Germany
[4] Univ Grenoble Alpes, IBS, CNRS, CEA, Grenoble, France
关键词
integrative structural biology; NMR; SAS; dynamics; protein complexes; X-RAY-SCATTERING; INTRINSICALLY DISORDERED PROTEINS; RESIDUAL DIPOLAR COUPLINGS; NUCLEAR-MAGNETIC-RESONANCE; MALATE-SYNTHASE-G; BIOLOGICAL MACROMOLECULES; MULTIDIMENSIONAL NMR; NEUTRON-SCATTERING; COMBINING NMR; MULTIDOMAIN PROTEINS;
D O I
10.1016/j.jmb.2020.03.014
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The study of complex and dynamic biomolecular assemblies is a key challenge in structural biology and requires the use of multiple methodologies providing complementary spatial and temporal information. NMR spectroscopy is a powerful technique that allows high-resolution structure determination of biomolecules as well as investigating their dynamic properties in solution. However, for high-molecular-weight systems, such as biomolecular complexes or multi-domain proteins, it is often only possible to obtain sparse NMR data, posing significant challenges to structure determination. Combining NMR data with information obtained from other solution techniques is therefore an attractive approach. The combination of NMR with small-angle X-ray and/or neutron scattering has been shown to be particularly fruitful. These scattering approaches provide low-resolution information of biomolecules in solution and reflect ensemble-averaged contributions of dynamic conformations for scattering molecules up to megadalton molecular weight. Here, we review recent developments in the combination of nuclear magnetic resonance spectroscopy (NMR) and small-angle scattering (SAS) experiments. We briefly outline the different types of information that are provided by these techniques. We then discuss computational methods that have been developed to integrate NMR and SAS data, particularly considering the presence of dynamic structural ensembles and flexibility of the investigated biomolecules. Finally, recent examples of the successful combination of NMR and SAS are presented to illustrate the utility of their combination. (C) 2020 Elsevier Ltd. All rights reserved.
引用
收藏
页码:2890 / 2912
页数:23
相关论文
共 250 条
  • [1] A further leap of improvement in tertiary structure prediction in CASP13 prompts new routes for future assessments
    Abriata, Luciano A.
    Tamo, Giorgio E.
    Dal Peraro, Matteo
    [J]. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2019, 87 (12) : 1100 - 1112
  • [2] [Anonymous], PROTEINS
  • [3] Bayesian inference of protein ensembles from SAXS data
    Antonov, L. D.
    Olsson, S.
    Boomsma, W.
    Hamelryck, T.
    [J]. PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 2016, 18 (08) : 5832 - 5838
  • [4] Proton-Detected Solid-State NMR Spectroscopy at Aliphatic Sites: Application to Crystalline Systems
    Asami, Sam
    Reif, Bernd
    [J]. ACCOUNTS OF CHEMICAL RESEARCH, 2013, 46 (09) : 2089 - 2097
  • [5] Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS
    Aznauryan, Mikayel
    Delgado, Leonildo
    Soranno, Andrea
    Nettels, Daniel
    Huang, Jie-rong
    Labhardt, Alexander M.
    Grzesiek, Stephan
    Schuler, Benjamin
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2016, 113 (37) : E5389 - E5398
  • [6] Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications
    Bah, Alaji
    Forman-Kay, Julie D.
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2016, 291 (13) : 6696 - 6705
  • [7] Sampling the conformational space of the catalytic subunit of human γ-secretase
    Bai, Xiao-chen
    Rajendra, Eeson
    Yang, Guanghui
    Shi, Yigong
    Scheres, Sjors H. W.
    [J]. ELIFE, 2015, 4
  • [8] How cryo-EM is revolutionizing structural biology
    Bai, Xiao-Chen
    McMullan, Greg
    Scheres, Sjors H. W.
    [J]. TRENDS IN BIOCHEMICAL SCIENCES, 2015, 40 (01) : 49 - 57
  • [9] Topological constraints: using RNA secondary structure to model 3D conformation, folding pathways, and dynamic adaptation
    Bailor, Maximillian H.
    Mustoe, Anthony M.
    Brooks, Charles L., III
    Al-Hashimi, Hashim M.
    [J]. CURRENT OPINION IN STRUCTURAL BIOLOGY, 2011, 21 (03) : 296 - 305
  • [10] Structure and mechanism of a molecular rheostat, an RNA thermometer that modulates immune evasion by Neisseria meningitidis
    Barnwal, Ravi Pratap
    Loh, Edmund
    Godin, Katherine S.
    Yip, Jordan
    Lavender, Hayley
    Tang, Christoph M.
    Varani, Gabriele
    [J]. NUCLEIC ACIDS RESEARCH, 2016, 44 (19) : 9426 - 9437