Postdoctoral Position in Biomolecular NMR of partially folded and intrinsically unfolded proteins at the Institute of Structural Biology in Grenoble, France.
Two year postdoctoral position to work in NMR developments for the study of partially folded proteins at the Institute of Structural Biology in Grenoble (in the group of Martin Blackledge : Protein Dynamics and Flexibility by NMR).
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Current research interests lie in the study of conformational flexibility in proteins in their different forms, from intrinsically disordered proteins to folded globular proteins, and to understand the complex relationship between molecular motion and biological function and malfunction. Our principal tool is Nuclear Magnetic Resonance (NMR), combined with complementary biophysical techniques such as molecular simulation and small angle scattering. We are actively collaborating with a number of groups, allowing immediate application of developed techniques to biological paradigms involving dynamic or disordered systems. The key systems that we are studying are proteins involved in the development of neurodegenerative disease, viral proteins regulating transcription and replication and cancer-related proteins. Some relevant references listed below.
The Institute of Structural Biology houses three NMR spectrometers equipped with cryogenic probes (two 600 MHz and one 800 MHz) and the group collaborates closely with the nearby European high field NMR centre in Lyon with access to higher field instruments (900 MHz and 1 GHz NMR spectrometers by the end 2008). The NMR groups at the IBS also share access to a fully equipped wet lab for the preparation of isotopically labeled NMR samples.
Grenoble is a pleasant city situated in the heart of the French Alps and hosts one of Europe’s most vibrant structural biology communities comprising the European Synchrotron Radiation Facility (ESRF), the Laue Langevin Institute (ILL), the Structural Biology Institute (IBS) and the EMBL Grenoble Out-Station.
Previous experience in the study of biomolecular structure or dynamics using modern heteronuclear NMR spectroscopy techniques is considered an advantage, although candidates from complementary fields will also be considered.
A competitive salary (based on previous research experience) is offered with health insurance, retirement plan and language training allowance. Interested candidates should forward a curriculum vitae, list of publication and electronic and postal addresses of potential referees to firstname.lastname@example.org
Quantitative Conformational Analysis of Partially Folded Proteins from Residual Dipolar Couplings : Application to the Molecular Recognition Element of Sendai Virus Nucleoprotein. Malene Ringkjøbing Jensen, Klaartje Houben, Ewen Lescop, Laurence Blanchard, Rob W.H. Ruigrok and Martin Blackledge. J.Am.Chem.Soc. 130, 8055-8061 (2008).
Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domainMark Wells, Henning Tidow, Trevor J. Rutherford, Phineus Markwick, Malene Ringkjobing Jensen, Efstratios Mylonas, Dmitri I. Svergun, Martin Blackledge*, and Alan R. Fersht*. Proc. Natl. Acad. Sci. (U.S.A.) 105, 5762–5767 (2008).
Mapping the Conformational Landscape of Urea-Denatured Ubiquitin using Residual Dipolar Couplings. Sebastian Meier, Stephan Grzesiek and Martin Blackledge J.Am.Chem.Soc. 129, 9799-9807 (2007).
Highly Populated Turn Conformations in Natively Unfolded Tau Protein Identified from Residual Dipolar Couplings and Molecular Simulation. M. D. Mukrasch, P.R.L. Markwick, J. Biernat, M. von Bergen, P. Bernado, C. Griesinger, E. Mandelkow, M. Zweckstetter and M. Blackledge J.Am.Chem.Soc. 129, 5235-5243 (2007).
Exploring Multiple Timescale Motions in Protein GB3 using Accelerated Molecular Dynamics and NMR. P. Markwick, G. Bouvignies and M. Blackledge J.Am.Chem.Soc. 129, 4724-4730 (2007).
Protein Dynamics and Flexibility by NMR
Institut de Biologie Structurale
41 Rue Jules Horowitz
Telephone: +33 438 789 554