TY - JOUR
T1 - Investigating the role of large-scale domain dynamics in protein-protein interactions
AU - Delaforge, Elise
AU - Milles, Sigrid
AU - Huang, Jie Rong
AU - Bouvier, Denis
AU - Jensen, Malene Ringkjøbing
AU - Sattler, Michael
AU - Hart, Darren J.
AU - Blackledge, Martin
N1 - Publisher Copyright:
© 2016 Delaforge, Milles, Huang, Bouvier, Jensen, Sattler, Hart and Blackledge.
PY - 2016/9/13
Y1 - 2016/9/13
N2 - 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.
AB - 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.
KW - Chemical exchange saturation transfer (CEST)
KW - Conformational dynamics
KW - Free-energy landscape
KW - Multi-domain proteins
KW - Nuclear magnetic resonance (NMR)
KW - Single molecule Förster resonance energy transfer (FRET)
KW - Small angle scattering
UR - http://www.scopus.com/inward/record.url?scp=85020742366&partnerID=8YFLogxK
U2 - 10.3389/fmolb.2016.00054
DO - 10.3389/fmolb.2016.00054
M3 - Short survey
AN - SCOPUS:85020742366
SN - 2296-889X
VL - 3
JO - Frontiers in Molecular Biosciences
JF - Frontiers in Molecular Biosciences
IS - SEP
M1 - 54
ER -