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WoS: 000985907400001
PMID: 37140345

Schanda, Paul. Research Data of the Publication “Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.” Institute of Science and Technology Austria, 2023, doi:10.15479/AT:ISTA:12820.
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Gauto, Diego F., et al. “Aromatic Ring Flips in Differently Packed Ubiquitin Protein Crystals from MAS NMR and MD.”10.1016/j.yjsbx.2022.100079__Journal of Structural Biology: X, vol. 7, 100079, Elsevier, 2023, doi:10.1016/j.yjsbx.2022.100079.
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Degen, Morris, et al. “Structural Basis of NINJ1-Mediated Plasma Membrane Rupture in Cell Death.”10.1038/s41586-023-05991-z__Nature, vol. 618, Springer Nature, 2023, pp. 1065–71, doi:10.1038/s41586-023-05991-z.
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Becker, Lea Marie, et al. “Cover Picture: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by MagicAngleSpinning NMR Spectroscopy of Aromatic Residues.”10.1002/anie.202304138__Angewandte Chemie International Edition, vol. 62, no. 19, e202304138, Wiley, 2023, doi:10.1002/anie.202304138.
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Becker, Lea Marie, et al. “Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – MagicAngleSpinning NMR Spektroskopie von aromatischen Resten.”10.1002/ange.202219314__Angewandte Chemie, vol. 135, no. 19, e202219314, Wiley, 2023, doi:10.1002/ange.202219314.
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Sudec, I., and Paul Schanda. “Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies.”10.1039/bk9781839165986-00136__Biophysics of Molecular Chaperones, edited by Sebastian Hiller et al., vol. 29, Royal Society of Chemistry, 2023, pp. 136–61, doi:10.1039/bk9781839165986-00136.
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Napoli, Federico, et al. “Protein Dynamics Detected by Magic-Angle Spinning Relaxation Dispersion NMR.”10.1016/j.sbi.2023.102660__Current Opinion in Structural Biology, vol. 82, no. 10, 102660, Elsevier, 2023, doi:10.1016/j.sbi.2023.102660.
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Becker, Lea Marie, et al. “The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by MagicAngle Spinning NMR of Aromatic Residues.”10.1002/anie.202219314__Angewandte Chemie International Edition, vol. 62, no. 19, e202219314, Wiley, 2023, doi:10.1002/anie.202219314.
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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. Institute of Science and Technology Austria, 2023, doi:10.15479/AT:ISTA:12497.
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Gauto, Diego F., et al. “Functional Control of a 0.5 MDa TET Aminopeptidase by a Flexible Loop Revealed by MAS NMR.”10.1038/s41467-022-29423-0__Nature Communications, vol. 13, 1927, Springer Nature, 2022, doi:10.1038/s41467-022-29423-0.
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Sudec, Iva, et al. “How Do Chaperones Bind (Partly) Unfolded Client Proteins?”10.3389/fmolb.2021.762005__Frontiers in Molecular Biosciences, vol. 8, 762005, Frontiers, 2021, doi:10.3389/fmolb.2021.762005.
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Rampelt, Heike, et al. “The Mitochondrial Carrier Pathway Transports Non-Canonical Substrates with an Odd Number of Transmembrane Segments.”10.1186/s12915-019-0733-6__BMC Biology, vol. 18, 2, Springer Nature, 2020, doi:10.1186/s12915-019-0733-6.
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Weinhäupl, Katharina, et al. “Architecture and Subunit Dynamics of the Mitochondrial TIM9·10·12 Chaperone.”10.1101/2020.03.13.990150__BioRxiv, Cold Spring Harbor Laboratory, doi:10.1101/2020.03.13.990150.
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Sudec, Iva, et al. “Structural Basis of Client Specificity in Mitochondrial Membrane-Protein Chaperones.”10.1101/2020.06.08.140772__BioRxiv, Cold Spring Harbor Laboratory, doi:10.1101/2020.06.08.140772.
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Gauto, Diego F., et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.”10.1038/s41467-019-10490-9__Nature Communications, vol. 10, 2697, Springer Nature, 2019, doi:10.1038/s41467-019-10490-9.
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Felix, Jan, et al. “Mechanism of the Allosteric Activation of the ClpP Protease Machinery by Substrates and Active-Site Inhibitors.”10.1126/sciadv.aaw3818__Science Advances, vol. 5, no. 9, ea, American Association for the Advancement of Science, 2019, doi:10.1126/sciadv.aaw3818.
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Rovó, Petra, et al. “Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.”10.1021/jacs.8b09258__Journal of the American Chemical Society, vol. 141, no. 2, American Chemical Society, 2019, pp. 858–69, doi:10.1021/jacs.8b09258.
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Shannon, Matthew D., et al. “Conformational Dynamics in the Core of Human 5Stop Prion Protein Amyloid Probed by Relaxation Dispersion NMR.”10.1002/cphc.201800779__ChemPhysChem, vol. 20, no. 2, Wiley, 2019, pp. 311–17, doi:10.1002/cphc.201800779.
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Marion, Dominique, et al. “Microsecond Protein Dynamics from Combined Bloch-McConnell and Near-Rotary-Resonance p Relaxation-Dispersion MAS NMR.”10.1002/cphc.201800935__ChemPhysChem, vol. 20, no. 2, Wiley, 2019, pp. 276–84, doi:10.1002/cphc.201800935.
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Bougault, Catherine, et al. “Studying Intact Bacterial Peptidoglycan by Proton-Detected NMR Spectroscopy at 100fkHz MAS Frequency.”10.1016/j.jsb.2018.07.009__Journal of Structural Biology, vol. 206, no. 1, Elsevier, 2019, pp. 66–72, doi:10.1016/j.jsb.2018.07.009.
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Schanda, Paul. “Relaxing with Liquids and Solids – A Perspective on Biomolecular Dynamics.”10.1016/j.jmr.2019.07.025__Journal of Magnetic Resonance, vol. 306, Elsevier, 2019, pp. 180–86, doi:10.1016/j.jmr.2019.07.025.
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Schanda, Paul, and Eduard Y. Chekmenev. “NMR for Biological Systems.”10.1002/cphc.201801100__ChemPhysChem, vol. 20, no. 2, Wiley, 2019, pp. 177–177, doi:10.1002/cphc.201801100.
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Gauto, Diego F., 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.”10.1021/jacs.9b04219__Journal of the American Chemical Society, vol. 141, no. 28, American Chemical Society, 2019, pp. 11183–95, doi:10.1021/jacs.9b04219.
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Kurauskas, Vilius, et al. “How Detergent Impacts Membrane Proteins: Atomic-Level Views of Mitochondrial Carriers in Dodecylphosphocholine.”10.1021/acs.jpclett.8b00269__The Journal of Physical Chemistry Letters, vol. 9, no. 5, American Chemical Society, 2018, pp. 933–38, doi:10.1021/acs.jpclett.8b00269.
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Weinhäupl, Katharina, et al. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain of Clp from Mycobacterium Tuberculosis.”10.1074/jbc.ra118.002251__Journal of Biological Chemistry, vol. 293, no. 22, American Society for Biochemistry &; Molecular Biology, 2018, pp. 8379–93, doi:10.1074/jbc.ra118.002251.
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Chipot, Christophe, et al. “Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.”10.1021/acs.chemrev.7b00570__Chemical Reviews, vol. 118, no. 7, American Chemical Society, 2018, pp. 3559–607, doi:10.1021/acs.chemrev.7b00570.
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Krushelnitsky, Alexey, et al. “Microsecond Motions Probed by Near-Rotary-Resonance <1 15N MAS NMR Experiments: The Model Case of Protein Overall-Rocking in Crystals.”10.1007/s10858-018-0191-4__Journal of Biomolecular NMR, vol. 71, no. 1, Springer Nature, 2018, pp. 53–67, doi:10.1007/s10858-018-0191-4.
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Laguri, Cedric, et al. “Solid State NMR Studies of Intact Lipopolysaccharide Endotoxin.”10.1021/acschembio.8b00271__ACS Chemical Biology, vol. 13, no. 8, American Chemical Society, 2018, pp. 2106–13, doi:10.1021/acschembio.8b00271.
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Mas, Guillaume, et al. “Structural Investigation of a Chaperonin in Action Reveals How Nucleotide Binding Regulates the Functional Cycle.”10.1126/sciadv.aau4196__Science Advances, vol. 4, no. 9, eaau4196, American Association for the Advancement of Science, 2018, doi:10.1126/sciadv.aau4196.
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Weinhäupl, Katharina, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.”10.1016/j.cell.2018.10.039__Cell, vol. 175, no. 5, Elsevier, 2018, p. 1365–1379.e25, doi:10.1016/j.cell.2018.10.039.
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Kurauskas, Vilius, et al. “Dynamics and Interactions of AA in DPC Are Not Functionally Relevant.”10.1038/s41594-018-0127-4__Nature Structural &; Molecular Biology, vol. 25, no. 9, Springer Nature, 2018, pp. 745–47, doi:10.1038/s41594-018-0127-4.
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Fraga, Hugo, et al. “Solidstate NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins.”10.1002/cphc.201700572__ChemPhysChem, vol. 18, no. 19, Wiley, 2017, pp. 2697–703, doi:10.1002/cphc.201700572.
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Kurauskas, Vilius, et al. “Slow Conformational Exchange and Overall Rocking Motion in Ubiquitin Protein Crystals.”10.1038/s41467-017-00165-8__Nature Communications, vol. 8, 145, Springer Nature, 2017, doi:10.1038/s41467-017-00165-8.
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Dehez, François, et al. “Mitochondrial ADP/ATP Carrier in Dodecylphosphocholine Binds Cardiolipins with Non-Native Affinity.”10.1016/j.bpj.2017.09.019__Biophysical Journal, vol. 113, no. 11, Elsevier, 2017, pp. 2311–15, doi:10.1016/j.bpj.2017.09.019.
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Rennella, Enrico, et al. “RNA Binding and Chaperone Activity of the E.Coli Cold-Shock Protein CspA.”10.1093/nar/gkx044__Nucleic Acids Research, vol. 45, no. 7, Oxford University Press, 2017, pp. 4255–68, doi:10.1093/nar/gkx044.
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Gauto, Diego F., et al. “Protein Conformational Dynamics Studied by 15N and 1H<1 Relaxation Dispersion: Application to Wild-Type and A Ubiquitin Crystals.”10.1016/j.ssnmr.2017.04.002__Solid State Nuclear Magnetic Resonance, vol. 87, no. 10, Elsevier, 2017, pp. 86–95, doi:10.1016/j.ssnmr.2017.04.002.
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Franco, Rémi, et al. “Optimized Fast Mixing Device for Real-Time NMR Applications.”10.1016/j.jmr.2017.05.016__Journal of Magnetic Resonance, vol. 281, no. 8, Elsevier, 2017, pp. 125–29, doi:10.1016/j.jmr.2017.05.016.
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Bersch, Beate, et al. “Proton-Detected Solid-State NMR Spectroscopy of a Zinc Diffusion Facilitator Protein in Native Nanodiscs.”10.1002/anie.201610441__Angewandte Chemie International Edition, vol. 56, no. 9, Wiley, 2017, pp. 2508–12, doi:10.1002/anie.201610441.
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Kurauskas, Vilius, et al. “Methyl-Specific Isotope Labeling Strategies for NMR Studies of Membrane Proteins.”10.1007/978-1-4939-7151-0_6__Membrane Protein Structure and Function Characterization, vol. 1635, Springer Nature, 2017, pp. 109–23, doi:10.1007/978-1-4939-7151-0_6.
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Kurauskas, Vilius, et al. “Sensitive Proton-Detected Solid-State NMR Spectroscopy of Large Proteins with Selective Clabelling: Application to the 50S Ribosome Subunit.”10.1039/c6cc04484k__Chemical Communications, vol. 52, no. 61, Royal Society of Chemistry, 2016, pp. 9558–61, doi:10.1039/c6cc04484k.
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Kurauskas, Vilius, et al. “Cross-Correlated Relaxation of Dipolar Coupling and Chemical-Shift Anisotropy in Magic-Angle Spinning <1 NMR Measurements: Application to Protein Backbone Dynamics Measurements.”10.1021/acs.jpcb.6b06129__The Journal of Physical Chemistry B, vol. 120, no. 34, American Chemical Society, 2016, pp. 8905–13, doi:10.1021/acs.jpcb.6b06129.
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Rodrigues, Christopher D. A., et al. “A Ring-Shaped Conduit Connects the Mother Cell and Forespore during Sporulation in Bacillus Subtilis.”10.1073/pnas.1609604113__Proceedings of the National Academy of Sciences, vol. 113, no. 41, National Academy of Sciences, 2016, pp. 11585–90, doi:10.1073/pnas.1609604113.
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Schanda, Paul, and Matthias Ernst. “Studying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules.”10.1016/j.pnmrs.2016.02.001__Progress in Nuclear Magnetic Resonance Spectroscopy, vol. 96, no. 8, Elsevier, 2016, pp. 1–46, doi:10.1016/j.pnmrs.2016.02.001.
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Ma, Peixiang, et al. “Observing the Overall Rocking Motion of a Protein in a Crystal.”10.1038/ncomms9361__Nature Communications, vol. 6, 8361, Springer Nature, 2015, doi:10.1038/ncomms9361.
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Ma, Peixiang, and Paul Schanda. “Conformational Exchange Processes in Biological Systems: Detection by Solid-State NMR.”10.1002/9780470034590.emrstm1418__EMagRes, vol. 4, no. 3, Wiley, 2015, pp. 699–708, doi:10.1002/9780470034590.emrstm1418.
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Morin, Sébastien, et al. “Relax: The Analysis of Biomolecular Kinetics and Thermodynamics Using NMR Relaxation Dispersion Data.”10.1093/bioinformatics/btu166__Bioinformatics, vol. 30, no. 15, Oxford University Press, 2014, pp. 2219–20, doi:10.1093/bioinformatics/btu166.
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Schanda, Paul, et al. “Atomic Model of a Cell-Wall Cross-Linking Enzyme in Complex with an Intact Bacterial Peptidoglycan.”10.1021/ja5105987__Journal of the American Chemical Society, vol. 136, no. 51, American Chemical Society, 2014, pp. 17852–60, doi:10.1021/ja5105987.
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Ma, Peixiang, et al. “Probing Transient Conformational States of Proteins by Solid-State <1 Relaxation-Dispersion NMR Spectroscopy.”10.1002/anie.201311275__Angewandte Chemie International Edition, vol. 53, no. 17, Wiley, 2014, pp. 4312–17, doi:10.1002/anie.201311275.
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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.”10.1007/s10858-013-9787-x__Journal of Biomolecular NMR, vol. 57, no. 3, Springer Nature, 2013, pp. 263–80, doi:10.1007/s10858-013-9787-x.
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Rennella, E., et al. “Oligomeric States along the Folding Pathways of -Microglobulin: Kinetics, Thermodynamics, and Structure.”10.1016/j.jmb.2013.04.028__Journal of Molecular Biology, vol. 425, no. 15, Elsevier, 2013, pp. 2722–36, doi:10.1016/j.jmb.2013.04.028.
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Asami, Sam, et al. “Optimal Degree of Protonation for 1H Detection of Aliphatic Sites in Randomly Deuterated Proteins as a Function of the MAS Frequency.”10.1007/s10858-012-9659-9__Journal of Biomolecular NMR, vol. 54, no. 2, Springer Nature, 2012, pp. 155–68, doi:10.1007/s10858-012-9659-9.
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Tollinger, Martin, et al. “Site-Resolved Measurement of Microsecond-to-Millisecond Conformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy.”10.1021/ja303591y__Journal of the American Chemical Society, vol. 134, no. 36, American Chemical Society, 2012, pp. 14800–07, doi:10.1021/ja303591y.
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Rennella, Enrico, et al. “Real-Time NMR Characterization of Structure and Dynamics in a Transiently Populated Protein Folding Intermediate.”10.1021/ja302598j__Journal of the American Chemical Society, vol. 134, no. 19, American Chemical Society, 2012, pp. 8066–69, doi:10.1021/ja302598j.
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Huber, Matthias, et al. “A Supplementary Coil for 2H Decoupling with Commercial HCN MAS Probes.”10.1016/j.jmr.2011.10.010__Journal of Magnetic Resonance, vol. 214, Elsevier, 2012, pp. 76–80, doi:10.1016/j.jmr.2011.10.010.
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Schanda, Paul, et al. “Accurate Measurement of One-Bond H–X Heteronuclear Dipolar Couplings in MAS Solid-State NMR.”10.1016/j.jmr.2011.03.015__Journal of Magnetic Resonance, vol. 210, no. 2, Elsevier, 2011, pp. 246–59, doi:10.1016/j.jmr.2011.03.015.
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Huber, Matthias, et al. “A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.”10.1002/cphc.201100062__ChemPhysChem, vol. 12, no. 5, Wiley, 2011, pp. 915–18, doi:10.1002/cphc.201100062.
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Schanda, Paul, et al. “Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.”10.1002/anie.201103944__Angewandte Chemie International Edition, vol. 50, no. 46, Wiley, 2011, pp. 11005–09, doi:10.1002/anie.201103944.
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Lalli, Daniela, et al. “Three-Dimensional Deuterium-Carbon Correlation Experiments for High-Resolution Solid-State MAS NMR Spectroscopy of Large Proteins.”10.1007/s10858-011-9578-1__Journal of Biomolecular NMR, vol. 51, no. 4, Springer Nature, 2011, pp. 477–85, doi:10.1007/s10858-011-9578-1.
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Van Melckebeke, Hélène, et al. “Probing Water Accessibility in HET-s(218–289) Amyloid Fibrils by Solid-State NMR.”10.1016/j.jmb.2010.11.004__Journal of Molecular Biology, vol. 405, no. 3, Elsevier, 2011, pp. 765–72, doi:10.1016/j.jmb.2010.11.004.
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DOI: 10.1016/j.jmb.2010.11.004

Corazza, Alessandra, et al. “Native-Unlike Long-Lived Intermediates along the Folding Pathway of the Amyloidogenic Protein -Microglobulin Revealed by Real-Time Two-Dimensional NMR.”10.1074/jbc.m109.061168__Journal of Biological Chemistry, vol. 285, no. 8, American Society for Biochemistry &; Molecular Biology, 2010, pp. 5827–35, doi:10.1074/jbc.m109.061168.
LibreCat: https://research-explorer.ista.ac.at/record/8473
DOI: 10.1074/jbc.m109.061168

Schanda, Paul, et al. “Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy.”10.1021/ja100726a__Journal of the American Chemical Society, vol. 132, no. 45, American Chemical Society, 2010, pp. 15957–67, doi:10.1021/ja100726a.
LibreCat: https://research-explorer.ista.ac.at/record/8472
DOI: 10.1021/ja100726a

Gal, Maayan, et al. “An Improved Ultrafast 2D NMR Experiment: Towards Atom-Resolved Real-Time Studies of Protein Kinetics at Multi-Hz Rates.”10.1007/s10858-008-9284-9__Journal of Biomolecular NMR, vol. 43, Springer Nature, 2009, pp. 1–10, doi:10.1007/s10858-008-9284-9.
LibreCat: https://research-explorer.ista.ac.at/record/8479
DOI: 10.1007/s10858-008-9284-9

Bruschweiler, Sven, et al. “Direct Observation of the Dynamic Process Underlying Allosteric Signal Transmission.”10.1021/ja809947w__Journal of the American Chemical Society, vol. 131, no. 8, American Chemical Society, 2009, pp. 3063–68, doi:10.1021/ja809947w.
LibreCat: https://research-explorer.ista.ac.at/record/8478
DOI: 10.1021/ja809947w

Farjon, Jonathan, et al. “Longitudinal-Relaxation-Enhanced NMR Experiments for the Study of Nucleic Acids in Solution.”10.1021/ja901633y__Journal of the American Chemical Society, vol. 131, no. 24, American Chemical Society, 2009, pp. 8571–77, doi:10.1021/ja901633y.
LibreCat: https://research-explorer.ista.ac.at/record/8476
DOI: 10.1021/ja901633y

Amero, Carlos, et al. “Fast Two-Dimensional NMR Spectroscopy of High Molecular Weight Protein Assemblies.”10.1021/ja809880p__Journal of the American Chemical Society, vol. 131, no. 10, American Chemical Society, 2009, pp. 3448–49, doi:10.1021/ja809880p.
LibreCat: https://research-explorer.ista.ac.at/record/8477
DOI: 10.1021/ja809880p

Schanda, Paul, et al. “Direct Detection of 3hJN’ Hydrogen-Bond Scalar Couplings in Proteins by Solid-State NMR Spectroscopy.”10.1002/anie.200904411__Angewandte Chemie International Edition, vol. 48, no. 49, Wiley, 2009, pp. 9322–25, doi:10.1002/anie.200904411.
LibreCat: https://research-explorer.ista.ac.at/record/8474
DOI: 10.1002/anie.200904411

Schanda, Paul. “Fast-Pulsing Longitudinal Relaxation Optimized Techniques: Enriching the Toolbox of Fast Biomolecular NMR Spectroscopy.”10.1016/j.pnmrs.2009.05.002__Progress in Nuclear Magnetic Resonance Spectroscopy, vol. 55, no. 3, Elsevier, 2009, pp. 238–65, doi:10.1016/j.pnmrs.2009.05.002.
LibreCat: https://research-explorer.ista.ac.at/record/8475
DOI: 10.1016/j.pnmrs.2009.05.002

Bersch, Beate, et al. “Molecular Structure and Metal-Binding Properties of the Periplasmic CopK Protein Expressed in Cupriavidus Metallidurans C during Copper Challenge.”10.1016/j.jmb.2008.05.017__Journal of Molecular Biology, vol. 380, no. 2, Elsevier, 2008, pp. 386–403, doi:10.1016/j.jmb.2008.05.017.
LibreCat: https://research-explorer.ista.ac.at/record/8481
DOI: 10.1016/j.jmb.2008.05.017

Schanda, Paul, et al. “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.”10.1016/j.jmb.2008.05.040__Journal of Molecular Biology, vol. 380, no. 4, Elsevier, 2008, pp. 726–41, doi:10.1016/j.jmb.2008.05.040.
LibreCat: https://research-explorer.ista.ac.at/record/8480
DOI: 10.1016/j.jmb.2008.05.040

Kern, Thomas, et al. “Sensitivity-Enhanced IPAP-SOFAST-HMQC for Fast-Pulsing 2D NMR with Reduced Radiofrequency Load.”10.1016/j.jmr.2007.11.015__Journal of Magnetic Resonance, vol. 190, no. 2, Elsevier, 2008, pp. 333–38, doi:10.1016/j.jmr.2007.11.015.
LibreCat: https://research-explorer.ista.ac.at/record/8482
DOI: 10.1016/j.jmr.2007.11.015

Schanda, Paul, et al. “Protein Folding and Unfolding Studied at Atomic Resolution by Fast Two-Dimensional NMR Spectroscopy.”10.1073/pnas.0702069104__Proceedings of the National Academy of Sciences, vol. 104, no. 27, National Academy of Sciences, 2007, pp. 11257–62, doi:10.1073/pnas.0702069104.
LibreCat: https://research-explorer.ista.ac.at/record/8483
DOI: 10.1073/pnas.0702069104

Gal, Maayan, et al. “UltraSOFAST HMQC NMR and the Repetitive Acquisition of 2D Protein Spectra at Hz Rates.”10.1021/ja066915g__Journal of the American Chemical Society, vol. 129, no. 5, American Chemical Society, 2007, pp. 1372–77, doi:10.1021/ja066915g.
LibreCat: https://research-explorer.ista.ac.at/record/8487
DOI: 10.1021/ja066915g

Schanda, Paul, et al. “Sensitivity-Optimized Experiment for the Measurement of Residual Dipolar Couplings between Amide Protons.”10.1007/s10858-006-9138-2__Journal of Biomolecular NMR, vol. 38, Springer Nature, 2007, pp. 47–55, doi:10.1007/s10858-006-9138-2.
LibreCat: https://research-explorer.ista.ac.at/record/8485
DOI: 10.1007/s10858-006-9138-2

Lescop, Ewen, et al. “Automated Spectral Compression for Fast Multidimensional NMR and Increased Time Resolution in Real-Time NMR Spectroscopy.”10.1021/ja068949u__Journal of the American Chemical Society, vol. 129, no. 10, American Chemical Society, 2007, pp. 2756–57, doi:10.1021/ja068949u.
LibreCat: https://research-explorer.ista.ac.at/record/8486
DOI: 10.1021/ja068949u

Lescop, Ewen, et al. “A Set of BEST Triple-Resonance Experiments for Time-Optimized Protein Resonance Assignment.”10.1016/j.jmr.2007.04.002__Journal of Magnetic Resonance, vol. 187, no. 1, Elsevier, 2007, pp. 163–69, doi:10.1016/j.jmr.2007.04.002.
LibreCat: https://research-explorer.ista.ac.at/record/8484
DOI: 10.1016/j.jmr.2007.04.002

Schanda, Paul, et al. “HET-SOFAST NMR for Fast Detection of Structural Compactness and Heterogeneity along Polypeptide Chains.”10.1002/mrc.1825__Magnetic Resonance in Chemistry, vol. 44, no. , Wiley, 2006, pp. 77–84, doi:10.1002/mrc.1825.
LibreCat: https://research-explorer.ista.ac.at/record/8489
DOI: 10.1002/mrc.1825

Schanda, Paul, et al. “Speeding up Three-Dimensional Protein NMR Experiments to a Few Minutes.”10.1021/ja062025p__Journal of the American Chemical Society, vol. 128, no. 28, American Chemical Society, 2006, pp. 9042–43, doi:10.1021/ja062025p.
LibreCat: https://research-explorer.ista.ac.at/record/8488
DOI: 10.1021/ja062025p

Schanda, Paul, and Bernhard Brutscher. “Hadamard Frequency-Encoded SOFAST-HMQC for Ultrafast Two-Dimensional Protein NMR.”10.1016/j.jmr.2005.10.007__Journal of Magnetic Resonance, vol. 178, no. 2, Elsevier, 2006, pp. 334–39, doi:10.1016/j.jmr.2005.10.007.
LibreCat: https://research-explorer.ista.ac.at/record/8490
DOI: 10.1016/j.jmr.2005.10.007

Schanda, Paul, et al. “SOFAST-HMQC Experiments for Recording Two-Dimensional Deteronuclear Correlation Spectra of Proteins within a Few Seconds.”10.1007/s10858-005-4425-x__Journal of Biomolecular NMR, vol. 33, no. 4, Springer Nature, 2005, pp. 199–211, doi:10.1007/s10858-005-4425-x.
LibreCat: https://research-explorer.ista.ac.at/record/8491
DOI: 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.”10.1021/ja051306e__Journal of the American Chemical Society, vol. 127, no. 22, American Chemical Society, 2005, pp. 8014–15, doi:10.1021/ja051306e.
LibreCat: https://research-explorer.ista.ac.at/record/8492
DOI: 10.1021/ja051306e