• J. Benesch (Oxford Univ. - UK): Weighing the quaternary dynamics of proteins.

 

• F. Bontems (ICSN- Gif-sur-Yvette – Fr.): Cost effective production of labeled proteins in insect cells for NMR studies. Application to class II viral fusion proteins.

 

• V. Brun (iRTSV- Grenoble- Fr) : Protein isotope-labelling and mass spectrometry analysis: Selected biomedical applications.

 

• R.A. Byrd (NIH-USA): Bio-orthogonal ¹⁹F Labeling  – New Approaches to ¹⁹F Methyl Labeling.

 

• T. Carlomagno (EMBL-Ger.): RNA-protein complexes in RNA metabolism: an integrative structure biology approach.

 

• M. Casiraghi (IBPC-Paris - Fr.) : Towards the detection of transiently formed G Protein–Coupled Receptor conformers in nanometric lipid bilayers by NMR spectroscopy.

 

• J. Chugh (Indian Institute of Science Education and Research - Pune): Visualizing Transient Structures in A-site RNA of the Ribosome: New Structures of Known Molecules for Drug Target.

 

• V. Dötsch (Franckfurt Univ. - Ger): New labeling approaches for the structure determination of membrane proteins.

 

• A. Duff (National Deuteration lab. – Australia): A robust and reliable method for high yield deuterated recombinant protein production using Escherichia coli BL21.

 

• L. Elantak (CNRS Marseille – Fr.): Galectin-1 dependent pre-B cell receptor activation.

 

• K. Gardner (CUNY - USA): NMR-based studies of bacterial signalling pathways: Insights into nature's view of the envirnment.

 

• A. Gossert (Novartis, CH): Affordable uniform isotope labeling with ²H, ¹³C and ¹⁵N in insect cells.

 

• M. Kainosho (Tokyo Univ.-Jap): Perspectives of the SAIL Method for Studying Structures and Dynamics of Larger Proteins.

 

• B. Kalodimos (Rutgers Univ.- USA): Determining structures of large dynamic protein complexes by NMR.

 

• S. Keane (HHMI- USA): Structure of the HIV-1 RNA Packaging Signal.
 

• C. Kreutz (Innsbruck Univ.- AT): Advanced stable isotope labeling methods for RNA NMR spectroscopy.
 

• C. Laguri (IBS – Grenoble – Fr.): Glycoconjugates isotopic labeling as tools to study cell surfaces and interactions of cells with their environment.

 

• I. Lebars (IGBMC- Strasbourg-Fr): A fully enzymatic method for site-directed spin labeling of long RNA.

 

• E. Lescop (ICSN Gif-sur-Yvette – Fr.): A well-balanced pre-existing equilibrium governs electron flux efficiency in a 70kDa diflavin reductase from NMR/SAXS combined techniques.

 

• R. Lichtenecker ( University of Vienna - Austria):  Isotope Labeled Precursors to be used in E. coli Protein Overexpression.

 

• P. Macek (IBS – Grenoble –Fr. /AstraZeneca UK): Unraveling Self-Assembly Pathways of Large Protein Machinery by Combining Time-Resolved EM, Native MS on Isotopically Hybridized Particle and Methyl-TROSY NMR.

 

• J. Markley (Madison Univ.-USA): Labeling strategies for NMR studies of interactions between nuclei and unpaired electrons in iron-sulfur proteins.

 

• G. Mas (IBS – Grenoble –Fr. ): Methyl specific Labelling, a tool to study a 1 MDa chaperonin in action.

 

• E. Michel (Zurich Univ. - Switzerland): Amino acid-selective segmental isotope labeling of multidomain proteins.

 

• Y. Monneau (Rutgers Univ.- USA/ IBS – Grenoble –Fr.): Development of non-stochastic and locally exhaustive search-based software to automatically assign ¹³C¹H resonances of methyl-labelled protein from 3D NOESY spectra and crystal structure.

 

• B. Odaert (CBMN – Bordeaux – Fr.): Initial steps in describing the F₁F_o ATP synthase dimer interface and modelling the small hydrophobic subunits of the F_o region with solution state NMR.

 

• A. Pedersen (Gothenburg Univ. - Sweden) : Improving amino acid incorporation efficiency with cell-free protein synthesis.

 

• A. Podjarny (IGBMC- Strasbourg-Fr): Solving biological puzzles using “tiny” perdeuterated crystals for subatomic resolution X-Ray and neutron diffraction.

 

• L. Ponchon (Univ. Paris V – Fr.): In vivo production of uniformally labelled RNA in Escherichia coli using a tRNA scaffold.

 

• P. Rajagopal (Washington Univ. – Seattle - USA): Hybrid Methodologies for Elucidating Structure and Function of a Chaperone.

 

• B. Reif (München Univ.- Ger): Amyloid aggregates and large soluble protein complexes.

 

• P. Schanda (IBS – Grenoble- Fr): - Seeing "invisible states" of proteins by MAS-NMR: new methods provide functional insight in a half-megadalton enzymatic assembly.

 

• T. Schubeis (Giotto Biotech – Florenze – Italy) : Segmental Isotope labelling of insoluble proteins for solid state NMR analysis.

 

• I. Shimada (Tokyo Univ.- Jap): Functional dynamics of GPCR in micelles and lipid bilayers.

 

• R. Sprangers (MPI-Ger): Obtaining high quality spectra of large asymmetric protein complexes: challenges and solutions.

 

• R. Sounier (IGF Montpellier – Fr.): Towards a mechanistic understanding of opioid receptors activation by liquid-state NMR spectroscopy.

 

• R. Trouillard (Rouen Univ; Fr): Production of uniformly ¹⁵N/¹³C labeled glycosylated proteins by hairy roots in view to NMR structural studies.

 

• V. Tugarinov (NIH-USA): Methyl Isotope Labeling in NMR Studies of Protein Dynamics, Allostery and Recognition.

 

• R. Walser (AstraZeneca UK) : Elucidating Structure and Function of a Nucleosome-Chromatin-Reader Complex.

 

• M. Weik (IBS – Grenoble- Fr) : Combining deuterium labelling and neutron spectroscopy to study protein and hydratation-water dynamics.

 

• J. Williamson (Scripps Institute-USA) : Dynamics of Ribosome Assembly in Bacteria.

 

• C. Wunderlich (Innsbruck Univ.-AT): Dynamics of naturally occurring methylated RNA building blocks probed by NMR spectroscopy.