Institut de Biologie StructuraleGrenoble / France

Contact person(s) related to this article / FAVIER Adrien / SCHANDA Paul


Publications of our team.

(Only a selection of the most recent articles is shown.)

Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan.
Paul Schanda, Sebastien Triboulet, Cedric Laguri, Catherine M Bougault, Isabel Ayala, Morgane Callon, Michel Arthur, and Jean-Pierre Simorre
J Am Chem Soc 2014, 136, 17852. link

relax: the analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data
Sébastien Morin, Troels E. Linnet, Mathilde Lescanne, Paul Schanda, Gary S. Thompson, Martin Tollinger, Kaare Teilum, Stéphane Gagné, Dominique Marion, Christian Griesinger, Martin Blackledge, Edward J. d’Auvergne
Bioinformatics link
doi: 10.1093/bioinformatics/btu166

Probing Transient Conformational States of Proteins by Solid-State R1ρ Relaxation-Dispersion NMR Spectroscopy
Ma P, Haller JD, Zajakala J, Macek P, Sivertsen AC, Willbold D, Boisbouvier J, Schanda P
Angewandte Chemie in press link
Ranked as "Very Important Paper" by the journal

Haller, J. and Schanda, P.
Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin
J Biomol NMR. 2013 Nov;57(3):263-80 link

Rennella, E., Cutuil, T., Schanda, P., Ayala, I., Gabel, F., Forge, V., Corazza, A., Esposito, E., Brutscher, B.
Oligomeric states along the folding pathways of b2-microglobulin: kinetics, thermodynamics, structure. J. Mol. Biol 425: 2722-36 (2013)


Huber, M., With, O., Schanda, P., Verel, R., Ernst, M., Meier, B. A supplementary coil for 2H decoupling with commercial HCN MAS probes. J. Magn. Reson. 214, 76-80 (2012)

Rennella, E., Cutuil, T., Schanda, P., Ayala, I., Forge, V., Brutscher, B. Real-Time NMR Characterization of Structure and Dynamics in a Transiently-Populated Protein Folding Intermediate. J. Am. Chem. Soc. 134: 8066-69 (2012)

Tollinger, M., Sivertsen, A. C., Meier, B. H., Ernst, M., Schanda, P. Site-resolved measurement of microsecond to millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy. J. Am. Chem. Soc. 134: 14800-07 (2012)
In this publication, we demonstrate for the first time the detection of low-populated excited states in proteins.

Asami S, Szekely K, Schanda P, Meier BH, Reif B. Optimal degree of protonation for H-1 detection of aliphatic sites in randomly deuterated proteins as a function of the MAS frequency. J. Biomol. NMR 54:155-68 (2012)


Van Melckebeke, H., Schanda, P., Gath, J., Wasmer, C., Verel, R., Lange, A., Meier, BH., Böckmann, A. Probing water accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR. J. Mol. Biol., 405, 765-72 (2011)

Huber, M., Hiller, S., Schanda, P., Ernst, M., Böckmann, A., Verel, R., Meier, BH. A proton-detected 4D solid-state NMR experiment for protein structure determination. ChemPhysChem, 12, 915-8 (2011)
I initiated this project and supervised the PhD student who finalized this work.

Schanda, P., Meier, BH., Ernst, M. Accurate measurement of one-bone H-X heteronuclear dipolar couplings in MAS solid-state NMR. J. Magn. Reson. 210, 246-59 (2011).

Schanda, P., Huber, M., Boisbouvier, J., Meier, BH., Ernst, M., Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion. Angew. Chem. Int. Ed. Engl. 50, 1105-9 (2011)

Lalli, D., Schanda, P., Chowdhury, A., Retel, J., Hiller, M., Higman, VA., Agarwal, V., Reif, B., van Rossum, B., Akbey, U., Oschkinat, H., Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins. J. Biomol. NMR, 51, 477-85 (2011)

Brutscher, B., Schanda, P. Rapid Multidimensional NMR: Fast-Pulsing Techniques and their Applications to Proteins. Encyclopedia of Magnetic Resonance. 43: 1-10 (2009). Book chapter.

Corazza, A., Rennella, E., Schanda, P., Mimmi, M.C., et al. Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic β2-microglobulin revealed by real-time 2D NMR. J. Biol. Chem., 285, 5827-35 (2010).

Schanda, P., Meier, B.H., Ernst, M. Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy. J. Am. Chem. Soc., 132, 15957-67 (2010).


Farjon, J., Boisbouvier, J., Schanda, P., Pardi, A., Simorre, J.P., Brutscher, B. Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution. J. Am. Chem. Soc. 131(24): 8571-7 (2009).

Amero, C., Schanda, P., Dura, M.A., Ayala, I., Marion, D., Franzetti, B., Brutscher, B., Boisbouvier, B. Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies. J. Am. Chem. Soc. 131(10): 3448-9 (2009).

Brüschweiler, S., Schanda, P., Kloiber, K., Brutscher, B., Kontaxis, G., Konrat, R., Tollinger, M. Direct observation of the dynamic process underlying allosteric signal transmission. J. Am. Chem. Soc. 131(8): 3063-68 (2009).

Gal, M., Kern, T., Schanda, P., Frydman, L., Brutscher, B. An improved ultrafast 2D NMR experiment: Toward atom-resolved real-time studies of protein kinetics at multi-Hz rates. J. Biomol. NMR. 43: 1-10 (2009).

Schanda, P. Fast-pulsing longitudinal relaxation optimized techniques: Enriching the toolbox of fast biomolecular NMR spectroscopy. Prog. NMR spectrosc. 55: 238-265 (2009).

Schanda, P., Huber, M., Verel, R., Ernst, M., Meier, B.H. Direct detection of 3hJNC’ hydrogen bond scalar couplings in proteins by solid-state NMR spectroscopy. Angew. Chem. Int. Ed. Engl., 49, 9322-9325 (2009).