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Delaforge, E.* ; Milles, S.* ; Huang, J.R.* ; Bouvier, D.* ; Jensen, M.R.* ; Sattler, M. ; Hart, D.J.* ; Blackledge, M.J.*

Investigating the role of large-scale domain dynamics in protein-protein interactions.

Front. Mol. Biosci. 3, 54 (2016)
Verlagsversion DOI
Open Access Gold
Creative Commons Lizenzvertrag
Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Schlagwörter Chemical Exchange Saturation Transfer (cest) ; Conformational Dynamics ; Free-energy Landscape ; Multi-domain Proteins ; Nuclear Magnetic Resonance (nmr) ; Single Molecule Förster Resonance Energy Transfer (fret) ; Small Angle Scattering
ISSN (print) / ISBN 2296-889X
e-ISSN 2296-889X
Quellenangaben Band: 3, Heft: , Seiten: 54 Artikelnummer: , Supplement: ,
Verlag Frontiers
Verlagsort Lausanne
Begutachtungsstatus Peer reviewed