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Hennig, J. ; Sattler, M.

The dynamic duo: Combining NMR and small angle scattering in structural biology.

Protein Sci. 23, 669-682 (2014)
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Structural biology provides essential information for elucidating molecular mechanisms that underlie biological function. Advances in hardware, sample preparation, experimental methods and computational approaches now enable structural analysis of protein complexes with increasing complexity that more closely represent biologically entities in the cellular environment. Integrated multi-disciplinary approaches are required to overcome limitations of individual methods and take advantage of complementary aspects provided by different structural biology techniques. Although X-ray crystallography remains the method of choice for structural analysis of large complexes, crystallization of flexible systems is often difficult and does typically not provide insights into conformational dynamics present in solution. Nuclear magnetic resonance spectroscopy (NMR) is on well-suited to study dynamics at picosecond to second time scales, and to map binding interfaces even of large systems at residue-resolution, but suffers from poor sensitivity with increasing molecular weight. Small angle scattering (SAS) methods provide low resolution information in solution and can characterize dynamics and conformational equilibria complementary to crystallography and NMR. The combination of NMR, crystallography and small angle scattering is thus very useful for analysis of the structure and conformational dynamics of (large) protein complexes in solution. In high molecular weight systems, where NMR data are often sparse, small angle scattering provides additional structural information and can differentiate between NMR-derived models. Scattering data can also validate the solution conformation of a crystal structure and indicate the presence of conformational equilibria. Here, we review current state-of-the-art approaches for combining NMR, crystallography and small angle scattering data to characterize protein complexes in solution.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Multi-domain Proteins ; Nmr ; Sans ; Saxs ; Structural Biology ; Protein Complexes; Residual Dipolar Couplings; X-ray-scattering; Intrinsically Disordered Proteins; Nuclear-magnetic-resonance; Molecular-weight Proteins; Global Fold Determination; Proton Relaxation Times; Site-directed Spin; Neutron-scattering; Functional Anthology
Language english
Publication Year 2014
HGF-reported in Year 2014
ISSN (print) / ISBN 0961-8368
e-ISSN 1469-896X
Journal Protein Science
Quellenangaben Volume: 23, Issue: 6, Pages: 669-682 Article Number: , Supplement: ,
Publisher Wiley
Publishing Place Hoboken
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-503000-001
PubMed ID 24687405
DOI 10.1002/pro.2467
WOS ID WOS:000336843100001
Scopus ID 84904170133
Erfassungsdatum 2014-04-03
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