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Combining NMR, SAXS and SANS to characterize the structure and dynamics of protein complexes.
Methods Enzymol. 678, 263-297 (2023)
Understanding the structure and dynamics of biological macromolecules is essential to decipher the molecular mechanisms that underlie cellular functions. The description of structure and conformational dynamics often requires the integration of complementary techniques. In this review, we highlight the utility of combining nuclear magnetic resonance (NMR) spectroscopy with small angle scattering (SAS) to characterize these challenging biomolecular systems. NMR can assess the structure and conformational dynamics of multidomain proteins, RNAs and biomolecular complexes. It can efficiently provide information on interaction surfaces, long-distance restraints and relative domain orientations at residue-level resolution. Such information can be readily combined with high-resolution structural data available on subcomponents of biomolecular assemblies. Moreover, NMR is a powerful tool to characterize the dynamics of biomolecules on a wide range of timescales, from nanoseconds to seconds. On the other hand, SAS approaches provide global information on the size and shape of biomolecules and on the ensemble of all conformations present in solution. Therefore, NMR and SAS provide complementary data that are uniquely suited to investigate dynamic biomolecular assemblies. Here, we briefly review the type of data that can be obtained by both techniques and describe different approaches that can be used to combine them to characterize biomolecular assemblies. We then provide guidelines on which experiments are best suited depending on the type of system studied, ranging from fully rigid complexes, dynamic structures that interconvert between defined conformations and systems with very high structural heterogeneity.
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Publication type
Article: Journal article
Document type
Review
Keywords
Dynamics ; Nmr ; Sans ; Saxs ; Small Angle Neutron Scattering ; Small Angle X-ray Scattering ; Structural Biology; Small-angle Scattering; X-ray-scattering; Automated Noe Assignment; Neutron-scattering; Chemical-exchange; Biological Macromolecules; Multidomain Proteins; Multidimensional Nmr; Secondary Structure; Rna-binding
ISSN (print) / ISBN
0076-6879
e-ISSN
0076-6879
Journal
Methods in Enzymology
Quellenangaben
Volume: 678,
Pages: 263-297
Publisher
Elsevier
Publishing Place
525 B Street, Suite 1900, San Diego, Ca 92101-4495 Usa
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
Grants
Helmholtz Association Initiative and Networking Fund
EU HORIZON 2020 research and innovation program under the Marie Sklodowska-Curie grant
EMBO Longterm Fellowship
Deutsche Forschungsgemeinschaft
EU HORIZON 2020 research and innovation program under the Marie Sklodowska-Curie grant
EMBO Longterm Fellowship
Deutsche Forschungsgemeinschaft