Protein Dynamics and Flexibility by NMR Group

Members

Permanent :

Martin Blackledge (Research director CEA) Google Scholar Profile

Malene Ringkjøbing Jensen (DR2 CNRS) Google Scholar Profile

Torsten Herrmann (DR2 CNRS) Google Scholar Profile UNIO Software

Sigrid Milles (CRCN CNRS)

Damien Maurin (Engineer CNRS)

Nicola Salvi (CEA researcher)

Non-permanent :

Wiktor Adamski (Ph.D. student)

Luiza Mamigonian Bessa (Postdoctoral fellow)

Aldo Camacho Zarcho (Postdoctoral fellow)

Serafima Guseva (Ph.D. student)

Anas Malki (Ph.D. student)

Thibault Orand (Ph.D. student)

Maud Tengo (research technician)

Presentation

Welcome to the web-page of the Protein Dynamics and Flexibility by NMR group at the IBS under the direction of Martin Blackledge. The overarching interest of our research group lies in the study of protein dynamics, developing and applying diverse experimental NMR and analytical approaches to characterize the role of conformational flexibility in biological function on a broad range of time and length scales, from molecular recognition dynamics in folded proteins, to reorganizational dynamics of large multidomain assemblies exhibiting extensive protein disorder.

Research topics

Our group is interested in :

• Intrinsically disordered proteins
• Protein domain dynamics
• Protein dynamics in the solid state
• Molecular recognition dynamics
• Intrinsic disorder in cell signalling

Key words

NMR, conformational flexibility, intrinsically disordered proteins, protein dynamics, protein structure determination, protein folding, functional dynamics.

Recent key publications

E. Delaforge, J. Kragelj, L. Tengo, A. Palencia, S. Milles, G. Bouvignies, N. Salvi, M. Blackledge and M.R. Jensen.
Deciphering the dynamic interaction profile of an intrinsically disordered protein by NMR exchange spectroscopy
J. Am. Chem. Soc. 140, 1148-1158 (2018).

N. Salvi, A. Abyzov and M. Blackledge.
Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins
Angew. Chem. 56, 14020-14024 (2017).

S. Milles, M.R. Jensen, G. Communie, D. Maurin, G. Schoehn, R.W. Ruigrok and M. Blackledge.
Self-assembly of measles virus nucleocapsid-like particles : Kinetics and RNA sequence Dependence
Angew. Chem. 55, 9356-9360 (2016).

A. Abyzov, N. Salvi, R. Schneider, D. Maurin, R.W. Ruigrok, M.R. Jensen and M. Blackledge.
Identification of dynamic modes in an intrinsically disordered protein using temperature-dependent NMR relaxation
J. Am. Chem. Soc. 138, 6240-6251 (2016).

S. Milles, D. Mercadante, I.V. Aramburu, M.R. Jensen, N. Banterle, C. Koehler, S. Tyagi, J. Clarke, S.L. Shamas, M. Blackledge*, F. Grater* and E.A. Lemke*.
Plasticity of an ultrafast interaction between nucleoporints and nuclear transport receptors
Cell 163, 734-745 (2015).

E. Delaforge, S. Milles, G. Bouvignies, D. Bouvier, S. Boivin, N. Salvi, D. Maurin, A. Round, E.A. Lemke, M.R. Jensen, D.J. Hart* and M. Blackledge*.
Large-scale conformational dynamics control H5N1 influenza polymerase PB2 binding to importin alpha
J. Am. Chem. Soc. 137, 15122-15134 (2015).

J.R. Lewandowski*, M.E. Halse, M. Blackledge* and L. Emsley*.
Direct observation of hierarchical protein dynamics.
Science 348, 578-581 (2015).

R. Schneider, D. Maurin, G. Communie G, J. Kragelj, D.F. Hansen, R.W. Ruigrok, M.R. Jensen and M. Blackledge.
Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR.
J. Am. Chem. Soc. 137, 1220-1229 (2015).

J. Huang, L. Warner, C. Sanchez, F. Gabel, T. Madl, C. Mackereth, M. Sattler* and M. Blackledge*.
Transient electrostatic interactions dominate the conformational equilibrium sampled by multidomain splicing factor U2AF65 : A combined NMR and SAXS study.
J. Am. Chem. Soc. 136, 7068-7076 (2014).

P. Guerry, L. Salmon, L. Mollica, J.L. Ortega Roldan, P. Markwick, N. van Nuland, J.A. McCammon and M. Blackledge
Mapping the population of protein conformational energy sub-states from NMR dipolar couplings.
Angew. Chem. 52, 3181-3185 (2013).

M. R. Jensen, G. Communie, E. A. Ribeiro, N. Martinez, A. Desfosses, L. Salmon, L. Mollica, F. Gabel, M. Jamin, S. Longhi, R. W. H. Ruigrok and M. Blackledge.
Intrinsic disorder in measles virus nucleocapsids.
Proc. Natl. Acad. Sci. (U.S.A.) 108, 9839-9844 (2011).

L. Salmon, G. Nodet, V. Ozenne, G. Yin, M. R. Jensen, M. Zweckstetter and M. Blackledge.
NMR characterization of long-range order in intrinsically disordered proteins.
J. Am. Chem. Soc. 132, 8407-8418 (2010).

M. R. Jensen*, L. Salmon, G. Nodet and M. Blackledge*.
Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts.
J. Am. Chem. Soc. 132, 1270-1272 (2010).

Updated 12/03/2018 by MRJ