PuSH - Publikationsserver des Helmholtz Zentrums München

Export: TXT Text RIS Endnote (RIS) BIB BibTeX
Hennig, J. ; Sattler, M.

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

Protein Sci. 23, 669-682 (2014)
Verlagsversion DOI PMC
Closed
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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.
Impact Factor
Scopus SNIP
Web of Science
Times Cited
Scopus
Cited By
Altmetric
2.861
0.820
32
40
Tags
Anmerkungen
Besondere Publikation
Auf Hompepage verbergern

Zusatzinfos bearbeiten
Eigene Tags bearbeiten
Privat
Eigene Anmerkung bearbeiten
Privat
Auf Publikationslisten für
Homepage nicht anzeigen
Als besondere Publikation
markieren
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter 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
Sprache englisch
Veröffentlichungsjahr 2014
HGF-Berichtsjahr 2014
ISSN (print) / ISBN 0961-8368
e-ISSN 1469-896X
Zeitschrift Protein Science
Quellenangaben Band: 23, Heft: 6, Seiten: 669-682 Artikelnummer: , Supplement: ,
Verlag Wiley
Verlagsort Hoboken
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
PubMed ID 24687405
DOI 10.1002/pro.2467
WOS ID WOS:000336843100001
Scopus ID 84904170133
Erfassungsdatum 2014-04-03
[➜Korrektur melden]