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Investigating the role of large-scale domain dynamics in protein-protein interactions.
Front. Mol. Biosci. 3, 54 (2016)
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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Publication type
Article: Journal article
Document type
Review
Keywords
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
Language
english
Publication Year
2016
HGF-reported in Year
2016
ISSN (print) / ISBN
2296-889X
e-ISSN
2296-889X
Quellenangaben
Volume: 3,
Pages: 54
Publisher
Frontiers
Publishing Place
Lausanne
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
27679800
Erfassungsdatum
2016-10-13