Institut de Biologie StructuraleGrenoble / France

Contact person(s) related to this article / BLACKLEDGE Martin

Protein Dynamics and Flexibility by NMR Group

Group leader : Martin Blackledge



Martin Blackledge (Research director CEA) Google Scholar Profile

Malene Ringkjøbing Jensen (CR1 CNRS) Google Scholar Profile

Sigrid Milles (CR2 CNRS)

Damien Maurin (Engineer CNRS)


Wictor Adamski (Ph.D. student)

Aldo Camacho Zarcho (Postdoctoral fellow)

Serafima Guseva (Ph.D. student)

Stefaniia Ivashchenko (Ph.D. student)

Nicola Salvi (Postdoctoral fellow)


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:

Key words

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

Key publications

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).

J. Kragelj, A. Palencia, M.H. Nanao, D. Maurin, G. Bouvignies, M. Blackledge* and M.R. Jensen*.
Structure and dynamics of the MKK7-JNK signaling complex.
Proc. Natl. Acad. Sci. (U.S.A.) 112, 3409-3414 (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).

V. Ozenne, R. Schneider, M. Yao, J.R. Huang, L. Salmon, M. Zweckstetter, M.R. Jensen and M. Blackledge
Mapping the potential energy landscape of intrinsically disordered proteins at amino acid resolution.
J. Am. Chem. Soc. 134, 15138-15148 (2012).

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).

L. Salmon, G. Bouvignies, P. Markwick, N. Lakomek, S. Showalter, D. W. Li, K. Walter, C. Griesinger, R. Bruschweiler and M. Blackledge.
Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: quantitative and absolute determination of backbone motion in ubiquitin.
Angew. Chem. 48, 4154-4157 (2009).

A full publication list of the FDP group since 2005 is available here.

[argent] Updated 21/04/2016 by MRJ[/argent]