Troussicot, Laura, Alicia Vallet, Mikael Molin, Björn M. Burmann, and Paul Schanda. “Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.”https://doi.org/10.1021/jacs.3c01200__Journal of the American Chemical Society. American Chemical Society, 2023.https://doi.org/10.1021/jacs.3c01200 .

Schanda, Paul. “Research Data of the Publication ‘Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.’”https://doi.org/10.15479/AT:ISTA:12820__Institute of Science and Technology Austria, 2023.https://doi.org/10.15479/AT:ISTA:12820 .

Gauto, Diego F., Olga O. Lebedenko, Lea Marie Becker, Isabel Ayala, Roman Lichtenecker, Nikolai R. Skrynnikov, and Paul Schanda. “Aromatic Ring Flips in Differently Packed Ubiquitin Protein Crystals from MAS NMR and MD.”https://doi.org/10.1016/j.yjsbx.2022.100079__Journal of Structural Biology: X. Elsevier, 2023.https://doi.org/10.1016/j.yjsbx.2022.100079 .

Degen, Morris, José Carlos Santos, Kristyna Pluhackova, Gonzalo Cebrero, Saray Ramos, Gytis Jankevicius, Ella Hartenian, et al. “Structural Basis of NINJ1-Mediated Plasma Membrane Rupture in Cell Death.”https://doi.org/10.1038/s41586-023-05991-z__Nature. Springer Nature, 2023.https://doi.org/10.1038/s41586-023-05991-z .

Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet, and Paul Schanda. Cover Picture: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by MagicAngleSpinning NMR Spectroscopy of Aromatic Residues. Angewandte Chemie International Edition. Vol. 62. Wiley, 2023.https://doi.org/10.1002/anie.202304138 .

Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet, and Paul Schanda. “Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – MagicAngleSpinning NMR Spektroskopie von aromatischen Resten.”https://doi.org/10.1002/ange.202219314__Angewandte Chemie. Wiley, 2023.https://doi.org/10.1002/ange.202219314 .

Sudec, I., and Paul Schanda. “Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies.”https://doi.org/10.1039/bk9781839165986-00136__In Biophysics of Molecular Chaperones, edited by Sebastian Hiller, Maili Liu, and Lichun He, 29:136–61. Royal Society of Chemistry, 2023.https://doi.org/10.1039/bk9781839165986-00136 .

Napoli, Federico, Lea Marie Becker, and Paul Schanda. “Protein Dynamics Detected by Magic-Angle Spinning Relaxation Dispersion NMR.”https://doi.org/10.1016/j.sbi.2023.102660__Current Opinion in Structural Biology. Elsevier, 2023.https://doi.org/10.1016/j.sbi.2023.102660 .

Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet, and Paul Schanda. “The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by MagicAngle Spinning NMR of Aromatic Residues.”https://doi.org/10.1002/anie.202219314__Angewandte Chemie International Edition. Wiley, 2023.https://doi.org/10.1002/anie.202219314 .

Becker, Lea Marie, and Paul Schanda. “Research Data to: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic-Angle-Spinning NMR Spectroscopy of Aromatic Residues.”https://doi.org/10.15479/AT:ISTA:12497__Institute of Science and Technology Austria, 2023.https://doi.org/10.15479/AT:ISTA:12497 .

Gauto, Diego F., Pavel Macek, Duccio Malinverni, Hugo Fraga, Matteo Paloni, Iva Sudec, Audrey Hessel, Juan Pablo Bustamante, Alessandro Barducci, and Paul Schanda. “Functional Control of a 0.5 MDa TET Aminopeptidase by a Flexible Loop Revealed by MAS NMR.”https://doi.org/10.1038/s41467-022-29423-0__Nature Communications. Springer Nature, 2022.https://doi.org/10.1038/s41467-022-29423-0 .

Sudec, Iva, Beate Bersch, and Paul Schanda. “How Do Chaperones Bind (Partly) Unfolded Client Proteins?”https://doi.org/10.3389/fmolb.2021.762005__Frontiers in Molecular Biosciences. Frontiers, 2021.https://doi.org/10.3389/fmolb.2021.762005 .

Rampelt, Heike, Iva Sucec, Beate Bersch, Patrick Horten, Inge Perschil, Jean-Claude Martinou, Martin van der Laan, Nils Wiedemann, Paul Schanda, and Nikolaus Pfanner. “The Mitochondrial Carrier Pathway Transports Non-Canonical Substrates with an Odd Number of Transmembrane Segments.”https://doi.org/10.1186/s12915-019-0733-6__BMC Biology. Springer Nature, 2020.https://doi.org/10.1186/s12915-019-0733-6 .

Weinhäupl, Katharina, Yong Wang, Audrey Hessel, Martha Brennich, Kresten Lindorff-Larsen, and Paul Schanda. “Architecture and Subunit Dynamics of the Mitochondrial TIM9·10·12 Chaperone.”https://doi.org/10.1101/2020.03.13.990150__BioRxiv. Cold Spring Harbor Laboratory, n.d.https://doi.org/10.1101/2020.03.13.990150 .

Sudec, Iva, Yong Wang, Ons Dakhlaoui, Katharina Weinhäupl, Tobias Jores, Doriane Costa, Audrey Hessel, et al. “Structural Basis of Client Specificity in Mitochondrial Membrane-Protein Chaperones.”https://doi.org/10.1101/2020.06.08.140772__BioRxiv. Cold Spring Harbor Laboratory, n.d.https://doi.org/10.1101/2020.06.08.140772 .

Gauto, Diego F., Leandro F. Estrozi, Charles D. Schwieters, Gregory Effantin, Pavel Macek, Remy Sounier, Astrid C. Sivertsen, et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.”https://doi.org/10.1038/s41467-019-10490-9__Nature Communications. Springer Nature, 2019.https://doi.org/10.1038/s41467-019-10490-9 .

Felix, Jan, Katharina Weinhäupl, Christophe Chipot, François Dehez, Audrey Hessel, Diego F. Gauto, Cecile Morlot, et al. “Mechanism of the Allosteric Activation of the ClpP Protease Machinery by Substrates and Active-Site Inhibitors.”https://doi.org/10.1126/sciadv.aaw3818__Science Advances. American Association for the Advancement of Science, 2019.https://doi.org/10.1126/sciadv.aaw3818 .

Rovó, Petra, Colin A. Smith, Diego Gauto, Bert L. de Groot, Paul Schanda, and Rasmus Linser. “Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.”https://doi.org/10.1021/jacs.8b09258__Journal of the American Chemical Society. American Chemical Society, 2019.https://doi.org/10.1021/jacs.8b09258 .

Shannon, Matthew D., Theint Theint, Dwaipayan Mukhopadhyay, Krystyna Surewicz, Witold K. Surewicz, Dominique Marion, Paul Schanda, and Christopher P. Jaroniec. “Conformational Dynamics in the Core of Human 5Stop Prion Protein Amyloid Probed by Relaxation Dispersion NMR.”https://doi.org/10.1002/cphc.201800779__ChemPhysChem. Wiley, 2019.https://doi.org/10.1002/cphc.201800779 .

Marion, Dominique, Diego F. Gauto, Isabel Ayala, Karine Giandoreggio-Barranco, and Paul Schanda. “Microsecond Protein Dynamics from Combined Bloch-McConnell and Near-Rotary-Resonance p Relaxation-Dispersion MAS NMR.”https://doi.org/10.1002/cphc.201800935__ChemPhysChem. Wiley, 2019.https://doi.org/10.1002/cphc.201800935 .

Bougault, Catherine, Isabel Ayala, Waldemar Vollmer, Jean-Pierre Simorre, and Paul Schanda. “Studying Intact Bacterial Peptidoglycan by Proton-Detected NMR Spectroscopy at 100fkHz MAS Frequency.”https://doi.org/10.1016/j.jsb.2018.07.009__Journal of Structural Biology. Elsevier, 2019.https://doi.org/10.1016/j.jsb.2018.07.009 .

Schanda, Paul. “Relaxing with Liquids and Solids – A Perspective on Biomolecular Dynamics.”https://doi.org/10.1016/j.jmr.2019.07.025__Journal of Magnetic Resonance. Elsevier, 2019.https://doi.org/10.1016/j.jmr.2019.07.025 .

Schanda, Paul, and Eduard Y. Chekmenev. “NMR for Biological Systems.”https://doi.org/10.1002/cphc.201801100__ChemPhysChem. Wiley, 2019.https://doi.org/10.1002/cphc.201801100 .

Gauto, Diego F., Pavel Macek, Alessandro Barducci, Hugo Fraga, Audrey Hessel, Tsutomu Terauchi, David Gajan, et al. “Aromatic Ring Dynamics, Thermal Activation, and Transient Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and Fast Magic-Angle Spinning NMR.”https://doi.org/10.1021/jacs.9b04219__Journal of the American Chemical Society. American Chemical Society, 2019.https://doi.org/10.1021/jacs.9b04219 .

Kurauskas, Vilius, Audrey Hessel, Peixiang Ma, Paola Lunetti, Katharina Weinhäupl, Lionel Imbert, Bernhard Brutscher, et al. “How Detergent Impacts Membrane Proteins: Atomic-Level Views of Mitochondrial Carriers in Dodecylphosphocholine.”https://doi.org/10.1021/acs.jpclett.8b00269__The Journal of Physical Chemistry Letters. American Chemical Society, 2018.https://doi.org/10.1021/acs.jpclett.8b00269 .

Weinhäupl, Katharina, Martha Brennich, Uli Kazmaier, Joel Lelievre, Lluis Ballell, Alfred Goldberg, Paul Schanda, and Hugo Fraga. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain of Clp from Mycobacterium Tuberculosis.”https://doi.org/10.1074/jbc.ra118.002251__Journal of Biological Chemistry. American Society for Biochemistry &; Molecular Biology, 2018.https://doi.org/10.1074/jbc.ra118.002251 .

Chipot, Christophe, François Dehez, Jason R. Schnell, Nicole Zitzmann, Eva Pebay-Peyroula, Laurent J. Catoire, Bruno Miroux, et al. “Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.”https://doi.org/10.1021/acs.chemrev.7b00570__Chemical Reviews. American Chemical Society, 2018.https://doi.org/10.1021/acs.chemrev.7b00570 .

Krushelnitsky, Alexey, Diego Gauto, Diana C. Rodriguez Camargo, Paul Schanda, and Kay Saalwächter. “Microsecond Motions Probed by Near-Rotary-Resonance <1 15N MAS NMR Experiments: The Model Case of Protein Overall-Rocking in Crystals.”https://doi.org/10.1007/s10858-018-0191-4__Journal of Biomolecular NMR. Springer Nature, 2018.https://doi.org/10.1007/s10858-018-0191-4 .

Laguri, Cedric, Alba Silipo, Alessandra M. Martorana, Paul Schanda, Roberta Marchetti, Alessandra Polissi, Antonio Molinaro, and Jean-Pierre Simorre. “Solid State NMR Studies of Intact Lipopolysaccharide Endotoxin.”https://doi.org/10.1021/acschembio.8b00271__ACS Chemical Biology. American Chemical Society, 2018.https://doi.org/10.1021/acschembio.8b00271 .

Mas, Guillaume, Jia-Ying Guan, Elodie Crublet, Elisa Colas Debled, Christine Moriscot, Pierre Gans, Guy Schoehn, Pavel Macek, Paul Schanda, and Jerome Boisbouvier. “Structural Investigation of a Chaperonin in Action Reveals How Nucleotide Binding Regulates the Functional Cycle.”https://doi.org/10.1126/sciadv.aau4196__Science Advances. American Association for the Advancement of Science, 2018.https://doi.org/10.1126/sciadv.aau4196 .

Weinhäupl, Katharina, Caroline Lindau, Audrey Hessel, Yong Wang, Conny Schütze, Tobias Jores, Laura Melchionda, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.”https://doi.org/10.1016/j.cell.2018.10.039__Cell. Elsevier, 2018.https://doi.org/10.1016/j.cell.2018.10.039 .

Kurauskas, Vilius, Audrey Hessel, François Dehez, Christophe Chipot, Beate Bersch, and Paul Schanda. “Dynamics and Interactions of AA in DPC Are Not Functionally Relevant.”https://doi.org/10.1038/s41594-018-0127-4__Nature Structural &; Molecular Biology. Springer Nature, 2018.https://doi.org/10.1038/s41594-018-0127-4 .

Fraga, Hugo, CharlesAdrien Arnaud, Diego F. Gauto, Maxime Audin, Vilius Kurauskas, Pavel Macek, Carsten Krichel, et al. “Solidstate NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins.”https://doi.org/10.1002/cphc.201700572__ChemPhysChem. Wiley, 2017.https://doi.org/10.1002/cphc.201700572 .

Kurauskas, Vilius, Sergei A. Izmailov, Olga N. Rogacheva, Audrey Hessel, Isabel Ayala, Joyce Woodhouse, Anastasya Shilova, et al. “Slow Conformational Exchange and Overall Rocking Motion in Ubiquitin Protein Crystals.”https://doi.org/10.1038/s41467-017-00165-8__Nature Communications. Springer Nature, 2017.https://doi.org/10.1038/s41467-017-00165-8 .

Dehez, François, Paul Schanda, Martin S. King, Edmund R.S. Kunji, and Christophe Chipot. “Mitochondrial ADP/ATP Carrier in Dodecylphosphocholine Binds Cardiolipins with Non-Native Affinity.”https://doi.org/10.1016/j.bpj.2017.09.019__Biophysical Journal. Elsevier, 2017.https://doi.org/10.1016/j.bpj.2017.09.019 .

Rennella, Enrico, Tomás Sára, Michael Juen, Christoph Wunderlich, Lionel Imbert, Zsofia Solyom, Adrien Favier, et al. “RNA Binding and Chaperone Activity of the E.Coli Cold-Shock Protein CspA.”https://doi.org/10.1093/nar/gkx044__Nucleic Acids Research. Oxford University Press, 2017.https://doi.org/10.1093/nar/gkx044 .

Gauto, Diego F., Audrey Hessel, Petra Rovó, Vilius Kurauskas, Rasmus Linser, and Paul Schanda. “Protein Conformational Dynamics Studied by 15N and 1H<1 Relaxation Dispersion: Application to Wild-Type and A Ubiquitin Crystals.”https://doi.org/10.1016/j.ssnmr.2017.04.002__Solid State Nuclear Magnetic Resonance. Elsevier, 2017.https://doi.org/10.1016/j.ssnmr.2017.04.002 .

Franco, Rémi, Adrien Favier, Paul Schanda, and Bernhard Brutscher. “Optimized Fast Mixing Device for Real-Time NMR Applications.”https://doi.org/10.1016/j.jmr.2017.05.016__Journal of Magnetic Resonance. Elsevier, 2017.https://doi.org/10.1016/j.jmr.2017.05.016 .

Bersch, Beate, Jonas M. Dörr, Audrey Hessel, J. Antoinette Killian, and Paul Schanda. “Proton-Detected Solid-State NMR Spectroscopy of a Zinc Diffusion Facilitator Protein in Native Nanodiscs.”https://doi.org/10.1002/anie.201610441__Angewandte Chemie International Edition. Wiley, 2017.https://doi.org/10.1002/anie.201610441 .

Kurauskas, Vilius, Paul Schanda, and Remy Sounier. “Methyl-Specific Isotope Labeling Strategies for NMR Studies of Membrane Proteins.”https://doi.org/10.1007/978-1-4939-7151-0_6__In Membrane Protein Structure and Function Characterization, 1635:109–23. Springer Nature, 2017.https://doi.org/10.1007/978-1-4939-7151-0_6 .

Kurauskas, Vilius, Elodie Crublet, Pavel Macek, Rime Kerfah, Diego F. Gauto, Jérôme Boisbouvier, and Paul Schanda. “Sensitive Proton-Detected Solid-State NMR Spectroscopy of Large Proteins with Selective Clabelling: Application to the 50S Ribosome Subunit.”https://doi.org/10.1039/c6cc04484k__Chemical Communications. Royal Society of Chemistry, 2016.https://doi.org/10.1039/c6cc04484k .

Kurauskas, Vilius, Emmanuelle Weber, Audrey Hessel, Isabel Ayala, Dominique Marion, and Paul Schanda. “Cross-Correlated Relaxation of Dipolar Coupling and Chemical-Shift Anisotropy in Magic-Angle Spinning <1 NMR Measurements: Application to Protein Backbone Dynamics Measurements.”https://doi.org/10.1021/acs.jpcb.6b06129__The Journal of Physical Chemistry B. American Chemical Society, 2016.https://doi.org/10.1021/acs.jpcb.6b06129 .

Rodrigues, Christopher D. A., Xavier Henry, Emmanuelle Neumann, Vilius Kurauskas, Laure Bellard, Yann Fichou, Paul Schanda, Guy Schoehn, David Z. Rudner, and Cecile Morlot. “A Ring-Shaped Conduit Connects the Mother Cell and Forespore during Sporulation in Bacillus Subtilis.”https://doi.org/10.1073/pnas.1609604113__Proceedings of the National Academy of Sciences. National Academy of Sciences, 2016.https://doi.org/10.1073/pnas.1609604113 .

Schanda, Paul, and Matthias Ernst. “Studying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules.”https://doi.org/10.1016/j.pnmrs.2016.02.001__Progress in Nuclear Magnetic Resonance Spectroscopy. Elsevier, 2016.https://doi.org/10.1016/j.pnmrs.2016.02.001 .

Ma, Peixiang, Yi Xue, Nicolas Coquelle, Jens D. Haller, Tairan Yuwen, Isabel Ayala, Oleg Mikhailovskii, et al. “Observing the Overall Rocking Motion of a Protein in a Crystal.”https://doi.org/10.1038/ncomms9361__Nature Communications. Springer Nature, 2015.https://doi.org/10.1038/ncomms9361 .

Ma, Peixiang, and Paul Schanda. “Conformational Exchange Processes in Biological Systems: Detection by Solid-State NMR.”https://doi.org/10.1002/9780470034590.emrstm1418__EMagRes. Wiley, 2015.https://doi.org/10.1002/9780470034590.emrstm1418 .

Morin, Sébastien, Troels E Linnet, Mathilde Lescanne, Paul Schanda, Gary S Thompson, Martin Tollinger, Kaare Teilum, et al. “Relax: The Analysis of Biomolecular Kinetics and Thermodynamics Using NMR Relaxation Dispersion Data.”https://doi.org/10.1093/bioinformatics/btu166__Bioinformatics. Oxford University Press, 2014.https://doi.org/10.1093/bioinformatics/btu166 .

Schanda, Paul, Sébastien Triboulet, Cédric Laguri, Catherine M. Bougault, Isabel Ayala, Morgane Callon, Michel Arthur, and Jean-Pierre Simorre. “Atomic Model of a Cell-Wall Cross-Linking Enzyme in Complex with an Intact Bacterial Peptidoglycan.”https://doi.org/10.1021/ja5105987__Journal of the American Chemical Society. American Chemical Society, 2014.https://doi.org/10.1021/ja5105987 .

Ma, Peixiang, Jens D. Haller, Jérémy Zajakala, Pavel Macek, Astrid C. Sivertsen, Dieter Willbold, Jérôme Boisbouvier, and Paul Schanda. “Probing Transient Conformational States of Proteins by Solid-State <1 Relaxation-Dispersion NMR Spectroscopy.”https://doi.org/10.1002/anie.201311275__Angewandte Chemie International Edition. Wiley, 2014.https://doi.org/10.1002/anie.201311275 .

Haller, Jens D., and Paul Schanda. “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.”https://doi.org/10.1007/s10858-013-9787-x__Journal of Biomolecular NMR. Springer Nature, 2013.https://doi.org/10.1007/s10858-013-9787-x .

Rennella, E., T. Cutuil, Paul Schanda, I. Ayala, F. Gabel, V. Forge, A. Corazza, G. Esposito, and B. Brutscher. “Oligomeric States along the Folding Pathways of -Microglobulin: Kinetics, Thermodynamics, and Structure.”https://doi.org/10.1016/j.jmb.2013.04.028__Journal of Molecular Biology. Elsevier, 2013.https://doi.org/10.1016/j.jmb.2013.04.028 .

Asami, Sam, Kathrin Szekely, Paul Schanda, Beat H. Meier, and Bernd Reif. “Optimal Degree of Protonation for 1H Detection of Aliphatic Sites in Randomly Deuterated Proteins as a Function of the MAS Frequency.”https://doi.org/10.1007/s10858-012-9659-9__Journal of Biomolecular NMR. Springer Nature, 2012.https://doi.org/10.1007/s10858-012-9659-9 .

Tollinger, Martin, Astrid C. Sivertsen, Beat H. Meier, Matthias Ernst, and Paul Schanda. “Site-Resolved Measurement of Microsecond-to-Millisecond Conformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy.”https://doi.org/10.1021/ja303591y__Journal of the American Chemical Society. American Chemical Society, 2012.https://doi.org/10.1021/ja303591y .

Rennella, Enrico, Thomas Cutuil, Paul Schanda, Isabel Ayala, Vincent Forge, and Bernhard Brutscher. “Real-Time NMR Characterization of Structure and Dynamics in a Transiently Populated Protein Folding Intermediate.”https://doi.org/10.1021/ja302598j__Journal of the American Chemical Society. American Chemical Society, 2012.https://doi.org/10.1021/ja302598j .

Huber, Matthias, Oliver With, Paul Schanda, René Verel, Matthias Ernst, and Beat H. Meier. “A Supplementary Coil for 2H Decoupling with Commercial HCN MAS Probes.”https://doi.org/10.1016/j.jmr.2011.10.010__Journal of Magnetic Resonance. Elsevier, 2012.https://doi.org/10.1016/j.jmr.2011.10.010 .

Schanda, Paul, Beat H. Meier, and Matthias Ernst. “Accurate Measurement of One-Bond H–X Heteronuclear Dipolar Couplings in MAS Solid-State NMR.”https://doi.org/10.1016/j.jmr.2011.03.015__Journal of Magnetic Resonance. Elsevier, 2011.https://doi.org/10.1016/j.jmr.2011.03.015 .

Huber, Matthias, Sebastian Hiller, Paul Schanda, Matthias Ernst, Anja Böckmann, René Verel, and Beat H. Meier. “A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.”https://doi.org/10.1002/cphc.201100062__ChemPhysChem. Wiley, 2011.https://doi.org/10.1002/cphc.201100062 .

Schanda, Paul, Matthias Huber, Jérôme Boisbouvier, Beat H. Meier, and Matthias Ernst. “Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.”https://doi.org/10.1002/anie.201103944__Angewandte Chemie International Edition. Wiley, 2011.https://doi.org/10.1002/anie.201103944 .

Lalli, Daniela, Paul Schanda, Anup Chowdhury, Joren Retel, Matthias Hiller, Victoria A. Higman, Lieselotte Handel, et al. “Three-Dimensional Deuterium-Carbon Correlation Experiments for High-Resolution Solid-State MAS NMR Spectroscopy of Large Proteins.”https://doi.org/10.1007/s10858-011-9578-1__Journal of Biomolecular NMR. Springer Nature, 2011.https://doi.org/10.1007/s10858-011-9578-1 .

Van Melckebeke, Hélène, Paul Schanda, Julia Gath, Christian Wasmer, René Verel, Adam Lange, Beat H. Meier, and Anja Böckmann. “Probing Water Accessibility in HET-s(218–289) Amyloid Fibrils by Solid-State NMR.”https://doi.org/10.1016/j.jmb.2010.11.004__Journal of Molecular Biology. Elsevier, 2011.https://doi.org/10.1016/j.jmb.2010.11.004 .

Corazza, Alessandra, Enrico Rennella, Paul Schanda, Maria Chiara Mimmi, Thomas Cutuil, Sara Raimondi, Sofia Giorgetti, et al. “Native-Unlike Long-Lived Intermediates along the Folding Pathway of the Amyloidogenic Protein -Microglobulin Revealed by Real-Time Two-Dimensional NMR.”https://doi.org/10.1074/jbc.m109.061168__Journal of Biological Chemistry. American Society for Biochemistry &; Molecular Biology, 2010.https://doi.org/10.1074/jbc.m109.061168 .

Schanda, Paul, Beat H. Meier, and Matthias Ernst. “Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy.”https://doi.org/10.1021/ja100726a__Journal of the American Chemical Society. American Chemical Society, 2010.https://doi.org/10.1021/ja100726a .

Gal, Maayan, Thomas Kern, Paul Schanda, Lucio Frydman, and Bernhard Brutscher. “An Improved Ultrafast 2D NMR Experiment: Towards Atom-Resolved Real-Time Studies of Protein Kinetics at Multi-Hz Rates.”https://doi.org/10.1007/s10858-008-9284-9__Journal of Biomolecular NMR. Springer Nature, 2009.https://doi.org/10.1007/s10858-008-9284-9 .

Bruschweiler, Sven, Paul Schanda, Karin Kloiber, Bernhard Brutscher, Georg Kontaxis, Robert Konrat, and Martin Tollinger. “Direct Observation of the Dynamic Process Underlying Allosteric Signal Transmission.”https://doi.org/10.1021/ja809947w__Journal of the American Chemical Society. American Chemical Society, 2009.https://doi.org/10.1021/ja809947w .

Farjon, Jonathan, Jerome Boisbouvier, Paul Schanda, Arthur Pardi, Jean-Pierre Simorre, and Bernhard Brutscher. “Longitudinal-Relaxation-Enhanced NMR Experiments for the Study of Nucleic Acids in Solution.”https://doi.org/10.1021/ja901633y__Journal of the American Chemical Society. American Chemical Society, 2009.https://doi.org/10.1021/ja901633y .

Amero, Carlos, Paul Schanda, M. Asuncion Dura, Isabel Ayala, Dominique Marion, Bruno Franzetti, Bernhard Brutscher, and Jerome Boisbouvier. “Fast Two-Dimensional NMR Spectroscopy of High Molecular Weight Protein Assemblies.”https://doi.org/10.1021/ja809880p__Journal of the American Chemical Society. American Chemical Society, 2009.https://doi.org/10.1021/ja809880p .

Schanda, Paul, Matthias Huber, RenÃ© Verel, Matthias Ernst, and Beatâ€…H. Meier. “Direct Detection of 3hJN’ Hydrogen-Bond Scalar Couplings in Proteins by Solid-State NMR Spectroscopy.”https://doi.org/10.1002/anie.200904411__Angewandte Chemie International Edition. Wiley, 2009.https://doi.org/10.1002/anie.200904411 .

Schanda, Paul. “Fast-Pulsing Longitudinal Relaxation Optimized Techniques: Enriching the Toolbox of Fast Biomolecular NMR Spectroscopy.”https://doi.org/10.1016/j.pnmrs.2009.05.002__Progress in Nuclear Magnetic Resonance Spectroscopy. Elsevier, 2009.https://doi.org/10.1016/j.pnmrs.2009.05.002 .

Bersch, Beate, Adrien Favier, Paul Schanda, Sébastien van Aelst, Tatiana Vallaeys, Jacques Covès, Max Mergeay, and Ruddy Wattiez. “Molecular Structure and Metal-Binding Properties of the Periplasmic CopK Protein Expressed in Cupriavidus Metallidurans C during Copper Challenge.”https://doi.org/10.1016/j.jmb.2008.05.017__Journal of Molecular Biology. Elsevier, 2008.https://doi.org/10.1016/j.jmb.2008.05.017 .

Schanda, Paul, Bernhard Brutscher, Robert Konrat, and Martin Tollinger. “Folding of the KIX Domain: Characterization of the Equilibrium Analog of a Folding Intermediate Using 15N/13C Relaxation Dispersion and Fast 1H/2H Amide Exchange NMR Spectroscopy.”https://doi.org/10.1016/j.jmb.2008.05.040__Journal of Molecular Biology. Elsevier, 2008.https://doi.org/10.1016/j.jmb.2008.05.040 .

Kern, Thomas, Paul Schanda, and Bernhard Brutscher. “Sensitivity-Enhanced IPAP-SOFAST-HMQC for Fast-Pulsing 2D NMR with Reduced Radiofrequency Load.”https://doi.org/10.1016/j.jmr.2007.11.015__Journal of Magnetic Resonance. Elsevier, 2008.https://doi.org/10.1016/j.jmr.2007.11.015 .

Schanda, Paul, V. Forge, and B. Brutscher. “Protein Folding and Unfolding Studied at Atomic Resolution by Fast Two-Dimensional NMR Spectroscopy.”https://doi.org/10.1073/pnas.0702069104__Proceedings of the National Academy of Sciences. National Academy of Sciences, 2007.https://doi.org/10.1073/pnas.0702069104 .

Gal, Maayan, Paul Schanda, Bernhard Brutscher, and Lucio Frydman. “UltraSOFAST HMQC NMR and the Repetitive Acquisition of 2D Protein Spectra at Hz Rates.”https://doi.org/10.1021/ja066915g__Journal of the American Chemical Society. American Chemical Society, 2007.https://doi.org/10.1021/ja066915g .

Schanda, Paul, Ewen Lescop, Mirjam Falge, Rémy Sounier, Jérôme Boisbouvier, and Bernhard Brutscher. “Sensitivity-Optimized Experiment for the Measurement of Residual Dipolar Couplings between Amide Protons.”https://doi.org/10.1007/s10858-006-9138-2__Journal of Biomolecular NMR. Springer Nature, 2007.https://doi.org/10.1007/s10858-006-9138-2 .

Lescop, Ewen, Paul Schanda, Rodolfo Rasia, and Bernhard Brutscher. “Automated Spectral Compression for Fast Multidimensional NMR and Increased Time Resolution in Real-Time NMR Spectroscopy.”https://doi.org/10.1021/ja068949u__Journal of the American Chemical Society. American Chemical Society, 2007.https://doi.org/10.1021/ja068949u .

Lescop, Ewen, Paul Schanda, and Bernhard Brutscher. “A Set of BEST Triple-Resonance Experiments for Time-Optimized Protein Resonance Assignment.”https://doi.org/10.1016/j.jmr.2007.04.002__Journal of Magnetic Resonance. Elsevier, 2007.https://doi.org/10.1016/j.jmr.2007.04.002 .

Schanda, Paul, Vincent Forge, and Bernhard Brutscher. “HET-SOFAST NMR for Fast Detection of Structural Compactness and Heterogeneity along Polypeptide Chains.”https://doi.org/10.1002/mrc.1825__Magnetic Resonance in Chemistry. Wiley, 2006.https://doi.org/10.1002/mrc.1825 .

Schanda, Paul, Hélène Van Melckebeke, and Bernhard Brutscher. “Speeding up Three-Dimensional Protein NMR Experiments to a Few Minutes.”https://doi.org/10.1021/ja062025p__Journal of the American Chemical Society. American Chemical Society, 2006.https://doi.org/10.1021/ja062025p .

Schanda, Paul, and Bernhard Brutscher. “Hadamard Frequency-Encoded SOFAST-HMQC for Ultrafast Two-Dimensional Protein NMR.”https://doi.org/10.1016/j.jmr.2005.10.007__Journal of Magnetic Resonance. Elsevier, 2006.https://doi.org/10.1016/j.jmr.2005.10.007 .

Schanda, Paul, riks Kupde, and Bernhard Brutscher. “SOFAST-HMQC Experiments for Recording Two-Dimensional Deteronuclear Correlation Spectra of Proteins within a Few Seconds.”https://doi.org/10.1007/s10858-005-4425-x__Journal of Biomolecular NMR. Springer Nature, 2005.https://doi.org/10.1007/s10858-005-4425-x .

Schanda, Paul, and Bernhard Brutscher. “Very Fast Two-Dimensional NMR Spectroscopy for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of Seconds.”https://doi.org/10.1021/ja051306e__Journal of the American Chemical Society. American Chemical Society, 2005.https://doi.org/10.1021/ja051306e .