Menu
Institut de Biologie StructuraleGrenoble / France

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

Publications

Publications of our team.


(Only a selection of the most recent articles is shown.)
2018
Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.
Chipot C, Dehez F, Schnell JR, Zitzmann N, Pebay-Peyroula E, Catoire LJ, Miroux B, Kunji ERS, Veglia G, Cross TA, Schanda P.
Chem Rev. link

How Detergent Impacts Membrane Proteins: Atomic-Level Views of Mitochondrial Carriers in Dodecylphosphocholine.
Kurauskas V, Hessel A, Ma P, Lunetti P, Weinhäupl K, Imbert L, Brutscher B, King MS, Sounier R, Dolce V, Kunji ERS, Capobianco L, Chipot C, Dehez F, Bersch B, Schanda P.
J Phys Chem Lett. link

2017
Bersch B, Dörr JM, Hessel A , Killian JA, Schanda P.
Proton-detected solid-state NMR spectroscopy of a zinc diffusion facilitator protein in native nanodiscs Angew Chem Int Ed Engl 56(9): 2508-12. link

Gauto, DF, Hessel, A, Rovo, P, Kurauskas, V, Linser, R, Schanda, P.
Protein conformational dynamics studied by 1H and 15N R1rho relaxation dispersion ssNMR: application to wild-type and G53A ubiquitin. Solid-state Nucl Magn Reson. link

Kurauskas, V, Izmailov SA, Rogacheva, ON, Hessel, A, Ayala, I, Woodhouse, J, Xue, Y, Yuwen T, Coquelle, N, Colletier, JP, Skrynnikov, NR, Schanda, P.
Slow conformational exchange and overall rocking motion in ubiquitin protein crystals
Nature Commun. link

Fraga H, Arnaud CA, Gauto DF, Audin M, Kurauskas V, Macek P, Krichel C, Guan JY, Boisbouvier J, Sprangers R, Breyton C, Schanda P. Solid-state NMR H-N-(C)-H and H-N-C-C 3D/4D correlation experiments for resonance assignment of large proteins, ChemPhysChem 18(19):2697-2703.

Dehez, F., Schanda, P.*, King, M. S., Kunji, E. R. S. & Chipot, C.* Mitochondrial ADP/ATP Carrier in Dodecylphosphocholine Binds Cardiolipins with Non-native Affinity Biophys. J. link

2016
Schanda P and Ernst M.
Studying dynamics by magic-angle-spinning NMR spectroscopy: principles and applications to biomolecules. Prog. Nucl. Magn. Reson. Spectr, 2016, 96:1-46.
A broad and in-depth review about the theory and applications of dynamics measurements by MAS NMR, which may well become a reference in the field.

Kurauskas V, Weber E, Hessel A, Ayala I, Marion D, Schanda P
Cross-correlated relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning R1ρ NMR measurements: Applications to protein backbone dynamics measurements. J. Phys. Chem. B, 2016, 120(34): 8905-13.

Kurauskas V, Crublet E, Macek P, Kerfah R, Boisbouvier J, Schanda P
Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit. Chem. Commun. 2016, 52, 9558-9561

Rodrigues CDA, Henry X, Neumann E, Kurauskas V, Bellard L, Fichou Y, Schanda P, Schoehn G, Rudner DZ, Morlot C
A ring-shaped conduit connects the mother cell and forespore during sporulation in Bacillus subtilis. Proc Natl Acad. Sci. USA. 113 (41): 11585–11590

2015
Ma P, Schanda P Conformational Exchange Processes in Biological Systems: Detection by Solid-State NMR. Encyclopedia in Magnetic Resonance, 4(3).

Ma P, Xue Y, Coquelle N, Haller JD, Yuwen T, Ayala I, Mikhailovskii O, Willbold D, Colletier JP, Skrynnikov NR, Schanda P.
Observing the overall rocking motion of a protein in a crystal. Nature Communications. 6, 8361 (2015) link

2014
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

2013
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)

2012

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)

2011

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)

2010
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).

2009

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).