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Delhommel, F. ; Martinez Lumbreras, S. ; Sattler, M.

Combining NMR, SAXS and SANS to characterize the structure and dynamics of protein complexes.

Methods Enzymol. 678, 263-297 (2023)
DOI PMC
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Schlagwörter 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
Sprache englisch
Veröffentlichungsjahr 2023
Prepublished im Jahr 2022
HGF-Berichtsjahr 2022
ISSN (print) / ISBN 0076-6879
e-ISSN 0076-6879
Zeitschrift Methods in Enzymology
Quellenangaben Band: 678, Heft: , Seiten: 263-297 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort 525 B Street, Suite 1900, San Diego, Ca 92101-4495 Usa
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Enabling and Novel Technologies
PSP-Element(e) G-503000-001
Förderungen Helmholtz Association Initiative and Networking Fund
EU HORIZON 2020 research and innovation program under the Marie Sklodowska-Curie grant
EMBO Longterm Fellowship
Deutsche Forschungsgemeinschaft
DOI 10.1016/bs.mie.2022.09.020
WOS ID 001101796000010
Scopus ID 85143533242
PubMed ID 36641211
Erfassungsdatum 2022-12-15
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