Institut de Biologie StructuraleGrenoble / France

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


Publications of our team.

Only a selection of our articles is shown below. All articles can be found HERE


Gauto DF, Estrozi LF, Schwieters CD, Effantin G, Macek P, Sounier R, Sivertsen AC, Schmidt E, Kerfah R, Colletier JP, Güntert P, Favier A, Schoehn G, Boisbouvier J, Schanda P
Structure determination of a half-megadalton aminopeptidase enzyme complex from an integrated NMR and cryo-EM approach
Nature Communications (2019) 10(1):2697Final

Gauto DF, Macek P, Hessel A, Barducci A, Fraga H, Takeda M, Lichtenecker R, Kainosho M, Schanda P*
Aromatic ring dynamics and excited states detected in a half-megadalton aminopeptidase by specific labeling and MAS NMR
J. Am. Chem. Soc. 2019. link

Felix J, Weinhäupl K, Chipot C, Dehez F, Hessel A, Gauto DF, Morlot C, Abian O, Gutsche I, Velazquez-Campoy A, Schanda P*, Fraga H.*
Mechanism of the allosteric activation of the ClpP protease machinery by active-site inhibitors.
In press in Science Advances. Preprint

Rovo P, Smith CA, Gauto DF, de Groot BL, Schanda P, Linser R.
Mechanistic insights into microsecond timescale protein motion using complementary solid-state NMR techniques
Journal of the American Chemical Society (2019) 141(2): 858-869 link


Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space
Weinhäupl K et al & Schanda P.
Cell link

Dynamics and interactions of AAC3 in DPC are not functionally relevant
Kurauskas V, Audrey Hessel, Francois Dehez, Christophe Chipot, Beate Bersch & Paul Schanda
Nature Structural & Molecular Biology link

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


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 Communications. 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


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


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


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)