Paul Schanda

Schanda Group

81 Publications

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[81]
2023 | Journal Article | IST-REx-ID: 13095 | OA
Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR
L. Troussicot, A. Vallet, M. Molin, B.M. Burmann, P. Schanda, Journal of the American Chemical Society 145 (2023) 10700–10711.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[80]
2023 | Research Data | IST-REx-ID: 12820 | OA
Research data of the publication "Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR"
P. Schanda, (2023).
[Published Version] View | Files available | DOI
 
[79]
2023 | Journal Article | IST-REx-ID: 12114 | OA
Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD
D.F. Gauto, O.O. Lebedenko, L.M. Becker, I. Ayala, R. Lichtenecker, N.R. Skrynnikov, P. Schanda, Journal of Structural Biology: X 7 (2023).
[Published Version] View | Files available | DOI | PubMed | Europe PMC
 
[78]
2023 | Journal Article | IST-REx-ID: 13096 | OA
Structural basis of NINJ1-mediated plasma membrane rupture in cell death
M. Degen, J.C. Santos, K. Pluhackova, G. Cebrero, S. Ramos, G. Jankevicius, E. Hartenian, U. Guillerm, S.A. Mari, B. Kohl, D.J. Müller, P. Schanda, T. Maier, C. Perez, C. Sieben, P. Broz, S. Hiller, Nature 618 (2023) 1065–1071.
[Published Version] View | Files available | DOI | WoS
 
[77]
2023 | Other Publication | IST-REx-ID: 14861 | OA
Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues
L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R. Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Cover Picture: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues, Wiley, 2023.
[Published Version] View | Files available | DOI | Download Published Version (ext.)
 
[76]
2023 | Journal Article | IST-REx-ID: 14835 | OA
Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten
L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R. Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Angewandte Chemie 135 (2023).
[Published Version] View | Files available | DOI
 
[75]
2023 | Book Chapter | IST-REx-ID: 14847 | OA
Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies
I. Sučec, P. Schanda, in:, S. Hiller, M. Liu, L. He (Eds.), Biophysics of Molecular Chaperones, Royal Society of Chemistry, 2023, pp. 136–161.
[Preprint] View | DOI | Download Preprint (ext.)
 
[74]
2023 | Journal Article | IST-REx-ID: 14036 | OA
Protein dynamics detected by magic-angle spinning relaxation dispersion NMR
F. Napoli, L.M. Becker, P. Schanda, Current Opinion in Structural Biology 82 (2023).
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[73]
2023 | Journal Article | IST-REx-ID: 12675 | OA
The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues
L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R. Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Angewandte Chemie International Edition 62 (2023).
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[72]
2023 | Research Data | IST-REx-ID: 12497 | OA
Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues
L.M. Becker, P. Schanda, (2023).
[Published Version] View | Files available | DOI
 
[71]
2022 | Journal Article | IST-REx-ID: 11179 | OA
Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR
D.F. Gauto, P. Macek, D. Malinverni, H. Fraga, M. Paloni, I. Sučec, A. Hessel, J.P. Bustamante, A. Barducci, P. Schanda, Nature Communications 13 (2022).
[Published Version] View | Files available | DOI | WoS
 
[70]
2021 | Journal Article | IST-REx-ID: 10323 | OA
How do chaperones bind (partly) unfolded client proteins?
I. Sučec, B. Bersch, P. Schanda, Frontiers in Molecular Biosciences 8 (2021).
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[69]
2020 | Journal Article | IST-REx-ID: 8402 | OA
The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments
H. Rampelt, I. Sucec, B. Bersch, P. Horten, I. Perschil, J.-C. Martinou, M. van der Laan, N. Wiedemann, P. Schanda, N. Pfanner, BMC Biology 18 (2020).
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[68]
2020 | Preprint | IST-REx-ID: 8404 | OA
Architecture and subunit dynamics of the mitochondrial TIM9·10·12 chaperone
K. Weinhäupl, Y. Wang, A. Hessel, M. Brennich, K. Lindorff-Larsen, P. Schanda, BioRxiv (n.d.).
[Preprint] View | DOI | Download Preprint (ext.)
 
[67]
2020 | Preprint | IST-REx-ID: 8403 | OA
Structural basis of client specificity in mitochondrial membrane-protein chaperones
I. Sučec, Y. Wang, O. Dakhlaoui, K. Weinhäupl, T. Jores, D. Costa, A. Hessel, M. Brennich, D. Rapaport, K. Lindorff-Larsen, B. Bersch, P. Schanda, BioRxiv (n.d.).
[Preprint] View | DOI | Download Preprint (ext.)
 
[66]
2019 | Journal Article | IST-REx-ID: 8405 | OA
Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex
D.F. Gauto, L.F. Estrozi, C.D. Schwieters, G. Effantin, P. Macek, R. Sounier, A.C. Sivertsen, E. Schmidt, R. Kerfah, G. Mas, J.-P. Colletier, P. Güntert, A. Favier, G. Schoehn, P. Schanda, J. Boisbouvier, Nature Communications 10 (2019).
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[65]
2019 | Journal Article | IST-REx-ID: 8406 | OA
Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors
J. Felix, K. Weinhäupl, C. Chipot, F. Dehez, A. Hessel, D.F. Gauto, C. Morlot, O. Abian, I. Gutsche, A. Velazquez-Campoy, P. Schanda, H. Fraga, Science Advances 5 (2019).
[Published Version] View | DOI | Download Published Version (ext.)
 
[64]
2019 | Journal Article | IST-REx-ID: 8413
Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques
P. Rovó, C.A. Smith, D. Gauto, B.L. de Groot, P. Schanda, R. Linser, Journal of the American Chemical Society 141 (2019) 858–869.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[63]
2019 | Journal Article | IST-REx-ID: 8412
Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR
M.D. Shannon, T. Theint, D. Mukhopadhyay, K. Surewicz, W.K. Surewicz, D. Marion, P. Schanda, C.P. Jaroniec, ChemPhysChem 20 (2019) 311–317.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[62]
2019 | Journal Article | IST-REx-ID: 8411
Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR
D. Marion, D.F. Gauto, I. Ayala, K. Giandoreggio-Barranco, P. Schanda, ChemPhysChem 20 (2019) 276–284.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[61]
2019 | Journal Article | IST-REx-ID: 8409
Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency
C. Bougault, I. Ayala, W. Vollmer, J.-P. Simorre, P. Schanda, Journal of Structural Biology 206 (2019) 66–72.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[60]
2019 | Journal Article | IST-REx-ID: 8407
Relaxing with liquids and solids – A perspective on biomolecular dynamics
P. Schanda, Journal of Magnetic Resonance 306 (2019) 180–186.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[59]
2019 | Journal Article | IST-REx-ID: 8410 | OA
NMR for Biological Systems
P. Schanda, E.Y. Chekmenev, ChemPhysChem 20 (2019) 177–177.
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[58]
2019 | Journal Article | IST-REx-ID: 8408
Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR
D.F. Gauto, P. Macek, A. Barducci, H. Fraga, A. Hessel, T. Terauchi, D. Gajan, Y. Miyanoiri, J. Boisbouvier, R. Lichtenecker, M. Kainosho, P. Schanda, Journal of the American Chemical Society 141 (2019) 11183–11195.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[57]
2018 | Journal Article | IST-REx-ID: 8443
How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine
V. Kurauskas, A. Hessel, P. Ma, P. Lunetti, K. Weinhäupl, L. Imbert, B. Brutscher, M.S. King, R. Sounier, V. Dolce, E.R.S. Kunji, L. Capobianco, C. Chipot, F. Dehez, B. Bersch, P. Schanda, The Journal of Physical Chemistry Letters 9 (2018) 933–938.
View | DOI
 
[56]
2018 | Journal Article | IST-REx-ID: 8440
The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis
K. Weinhäupl, M. Brennich, U. Kazmaier, J. Lelievre, L. Ballell, A. Goldberg, P. Schanda, H. Fraga, Journal of Biological Chemistry 293 (2018) 8379–8393.
View | DOI
 
[55]
2018 | Journal Article | IST-REx-ID: 8442
Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies
C. Chipot, F. Dehez, J.R. Schnell, N. Zitzmann, E. Pebay-Peyroula, L.J. Catoire, B. Miroux, E.R.S. Kunji, G. Veglia, T.A. Cross, P. Schanda, Chemical Reviews 118 (2018) 3559–3607.
View | DOI
 
[54]
2018 | Journal Article | IST-REx-ID: 8441
Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals
A. Krushelnitsky, D. Gauto, D.C. Rodriguez Camargo, P. Schanda, K. Saalwächter, Journal of Biomolecular NMR 71 (2018) 53–67.
[Published Version] View | DOI
 
[53]
2018 | Journal Article | IST-REx-ID: 8439
Solid state NMR studies of intact lipopolysaccharide endotoxin
C. Laguri, A. Silipo, A.M. Martorana, P. Schanda, R. Marchetti, A. Polissi, A. Molinaro, J.-P. Simorre, ACS Chemical Biology 13 (2018) 2106–2113.
View | DOI
 
[52]
2018 | Journal Article | IST-REx-ID: 8437
Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle
G. Mas, J.-Y. Guan, E. Crublet, E.C. Debled, C. Moriscot, P. Gans, G. Schoehn, P. Macek, P. Schanda, J. Boisbouvier, Science Advances 4 (2018).
View | DOI
 
[51]
2018 | Journal Article | IST-REx-ID: 8436
Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space
K. Weinhäupl, C. Lindau, A. Hessel, Y. Wang, C. Schütze, T. Jores, L. Melchionda, B. Schönfisch, H. Kalbacher, B. Bersch, D. Rapaport, M. Brennich, K. Lindorff-Larsen, N. Wiedemann, P. Schanda, Cell 175 (2018) 1365–1379.e25.
View | DOI
 
[50]
2018 | Journal Article | IST-REx-ID: 8438
Dynamics and interactions of AAC3 in DPC are not functionally relevant
V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, P. Schanda, Nature Structural & Molecular Biology 25 (2018) 745–747.
View | DOI
 
[49]
2017 | Journal Article | IST-REx-ID: 8446
Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins
H. Fraga, C. Arnaud, D.F. Gauto, M. Audin, V. Kurauskas, P. Macek, C. Krichel, J. Guan, J. Boisbouvier, R. Sprangers, C. Breyton, P. Schanda, ChemPhysChem 18 (2017) 2697–2703.
View | DOI
 
[48]
2017 | Journal Article | IST-REx-ID: 8445
Slow conformational exchange and overall rocking motion in ubiquitin protein crystals
V. Kurauskas, S.A. Izmailov, O.N. Rogacheva, A. Hessel, I. Ayala, J. Woodhouse, A. Shilova, Y. Xue, T. Yuwen, N. Coquelle, J.-P. Colletier, N.R. Skrynnikov, P. Schanda, Nature Communications 8 (2017).
[Published Version] View | DOI
 
[47]
2017 | Journal Article | IST-REx-ID: 8444
Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity
F. Dehez, P. Schanda, M.S. King, E.R.S. Kunji, C. Chipot, Biophysical Journal 113 (2017) 2311–2315.
View | DOI
 
[46]
2017 | Journal Article | IST-REx-ID: 8449
RNA binding and chaperone activity of the E.coli cold-shock protein CspA
E. Rennella, T. Sára, M. Juen, C. Wunderlich, L. Imbert, Z. Solyom, A. Favier, I. Ayala, K. Weinhäupl, P. Schanda, R. Konrat, C. Kreutz, B. Brutscher, Nucleic Acids Research 45 (2017) 4255–4268.
View | DOI
 
[45]
2017 | Journal Article | IST-REx-ID: 8447
Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals
D.F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, P. Schanda, Solid State Nuclear Magnetic Resonance 87 (2017) 86–95.
View | DOI
 
[44]
2017 | Journal Article | IST-REx-ID: 8448
Optimized fast mixing device for real-time NMR applications
R. Franco, A. Favier, P. Schanda, B. Brutscher, Journal of Magnetic Resonance 281 (2017) 125–129.
View | DOI
 
[43]
2017 | Journal Article | IST-REx-ID: 8451
Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native nanodiscs
B. Bersch, J.M. Dörr, A. Hessel, J.A. Killian, P. Schanda, Angewandte Chemie International Edition 56 (2017) 2508–2512.
View | DOI
 
[42]
2017 | Book Chapter | IST-REx-ID: 8450
Methyl-specific isotope labeling strategies for NMR studies of membrane proteins
V. Kurauskas, P. Schanda, R. Sounier, in:, Membrane Protein Structure and Function Characterization, Springer Nature, 2017, pp. 109–123.
View | DOI
 
[41]
2016 | Journal Article | IST-REx-ID: 8455
Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit
V. Kurauskas, E. Crublet, P. Macek, R. Kerfah, D.F. Gauto, J. Boisbouvier, P. Schanda, Chemical Communications 52 (2016) 9558–9561.
View | DOI
 
[40]
2016 | Journal Article | IST-REx-ID: 8453
Cross-correlated relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning R1ρ NMR measurements: Application to protein backbone dynamics measurements
V. Kurauskas, E. Weber, A. Hessel, I. Ayala, D. Marion, P. Schanda, The Journal of Physical Chemistry B 120 (2016) 8905–8913.
View | DOI
 
[39]
2016 | Journal Article | IST-REx-ID: 8452
A ring-shaped conduit connects the mother cell and forespore during sporulation in Bacillus subtilis
C.D.A. Rodrigues, X. Henry, E. Neumann, V. Kurauskas, L. Bellard, Y. Fichou, P. Schanda, G. Schoehn, D.Z. Rudner, C. Morlot, Proceedings of the National Academy of Sciences 113 (2016) 11585–11590.
View | DOI
 
[38]
2016 | Journal Article | IST-REx-ID: 8454
Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules
P. Schanda, M. Ernst, Progress in Nuclear Magnetic Resonance Spectroscopy 96 (2016) 1–46.
View | DOI
 
[37]
2015 | Journal Article | IST-REx-ID: 8456
Observing the overall rocking motion of a protein in a crystal
P. Ma, Y. Xue, N. Coquelle, J.D. Haller, T. Yuwen, I. Ayala, O. Mikhailovskii, D. Willbold, J.-P. Colletier, N.R. Skrynnikov, P. Schanda, Nature Communications 6 (2015).
[Published Version] View | DOI
 
[36]
2015 | Journal Article | IST-REx-ID: 8457
Conformational exchange processes in biological systems: Detection by solid-state NMR
P. Ma, P. Schanda, EMagRes 4 (2015) 699–708.
View | DOI
 
[35]
2014 | Journal Article | IST-REx-ID: 8459
Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data
S. Morin, T.E. Linnet, M. Lescanne, P. Schanda, G.S. Thompson, M. Tollinger, K. Teilum, S. Gagné, D. Marion, C. Griesinger, M. Blackledge, E.J. d’Auvergne, Bioinformatics 30 (2014) 2219–2220.
View | Files available | DOI
 
[34]
2014 | Journal Article | IST-REx-ID: 8458
Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan
P. Schanda, S. Triboulet, C. Laguri, C.M. Bougault, I. Ayala, M. Callon, M. Arthur, J.-P. Simorre, Journal of the American Chemical Society 136 (2014) 17852–17860.
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[33]
2014 | Journal Article | IST-REx-ID: 8460
Probing transient conformational states of proteins by solid-state R1ρ relaxation-dispersion NMR spectroscopy
P. Ma, J.D. Haller, J. Zajakala, P. Macek, A.C. Sivertsen, D. Willbold, J. Boisbouvier, P. Schanda, Angewandte Chemie International Edition 53 (2014) 4312–4317.
View | DOI
 
[32]
2013 | Journal Article | IST-REx-ID: 8461
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.D. Haller, P. Schanda, Journal of Biomolecular NMR 57 (2013) 263–280.
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[31]
2013 | Journal Article | IST-REx-ID: 8462
Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure
E. Rennella, T. Cutuil, P. Schanda, I. Ayala, F. Gabel, V. Forge, A. Corazza, G. Esposito, B. Brutscher, Journal of Molecular Biology 425 (2013) 2722–2736.
View | DOI
 
[30]
2012 | Journal Article | IST-REx-ID: 8463
Optimal degree of protonation for 1H detection of aliphatic sites in randomly deuterated proteins as a function of the MAS frequency
S. Asami, K. Szekely, P. Schanda, B.H. Meier, B. Reif, Journal of Biomolecular NMR 54 (2012) 155–168.
View | DOI
 
[29]
2012 | Journal Article | IST-REx-ID: 8465
Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy
M. Tollinger, A.C. Sivertsen, B.H. Meier, M. Ernst, P. Schanda, Journal of the American Chemical Society 134 (2012) 14800–14807.
View | DOI
 
[28]
2012 | Journal Article | IST-REx-ID: 8466
Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate
E. Rennella, T. Cutuil, P. Schanda, I. Ayala, V. Forge, B. Brutscher, Journal of the American Chemical Society 134 (2012) 8066–8069.
View | DOI
 
[27]
2012 | Journal Article | IST-REx-ID: 8467
A supplementary coil for 2H decoupling with commercial HCN MAS probes
M. Huber, O. With, P. Schanda, R. Verel, M. Ernst, B.H. Meier, Journal of Magnetic Resonance 214 (2012) 76–80.
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[26]
2011 | Journal Article | IST-REx-ID: 8469
Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR
P. Schanda, B.H. Meier, M. Ernst, Journal of Magnetic Resonance 210 (2011) 246–259.
View | DOI
 
[25]
2011 | Journal Article | IST-REx-ID: 8470
A proton-detected 4D solid-state NMR experiment for protein structure determination
M. Huber, S. Hiller, P. Schanda, M. Ernst, A. Böckmann, R. Verel, B.H. Meier, ChemPhysChem 12 (2011) 915–918.
View | DOI
 
[24]
2011 | Journal Article | IST-REx-ID: 8464
Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion
P. Schanda, M. Huber, J. Boisbouvier, B.H. Meier, M. Ernst, Angewandte Chemie International Edition 50 (2011) 11005–11009.
View | Files available | DOI
 
[23]
2011 | Journal Article | IST-REx-ID: 8468
Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins
D. Lalli, P. Schanda, A. Chowdhury, J. Retel, M. Hiller, V.A. Higman, L. Handel, V. Agarwal, B. Reif, B. van Rossum, Ü. Akbey, H. Oschkinat, Journal of Biomolecular NMR 51 (2011) 477–485.
View | DOI
 
[22]
2011 | Journal Article | IST-REx-ID: 8471
Probing water accessibility in HET-s(218–289) amyloid fibrils by solid-state NMR
H. Van Melckebeke, P. Schanda, J. Gath, C. Wasmer, R. Verel, A. Lange, B.H. Meier, A. Böckmann, Journal of Molecular Biology 405 (2011) 765–772.
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[21]
2010 | Journal Article | IST-REx-ID: 8473
Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR
A. Corazza, E. Rennella, P. Schanda, M.C. Mimmi, T. Cutuil, S. Raimondi, S. Giorgetti, F. Fogolari, P. Viglino, L. Frydman, M. Gal, V. Bellotti, B. Brutscher, G. Esposito, Journal of Biological Chemistry 285 (2010) 5827–5835.
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[20]
2010 | Journal Article | IST-REx-ID: 8472
Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy
P. Schanda, B.H. Meier, M. Ernst, Journal of the American Chemical Society 132 (2010) 15957–15967.
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[19]
2009 | Journal Article | IST-REx-ID: 8479
An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates
M. Gal, T. Kern, P. Schanda, L. Frydman, B. Brutscher, Journal of Biomolecular NMR 43 (2009) 1–10.
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[18]
2009 | Journal Article | IST-REx-ID: 8478
Direct observation of the dynamic process underlying allosteric signal transmission
S. Brüschweiler, P. Schanda, K. Kloiber, B. Brutscher, G. Kontaxis, R. Konrat, M. Tollinger, Journal of the American Chemical Society 131 (2009) 3063–3068.
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[17]
2009 | Journal Article | IST-REx-ID: 8476
Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution
J. Farjon, J. Boisbouvier, P. Schanda, A. Pardi, J.-P. Simorre, B. Brutscher, Journal of the American Chemical Society 131 (2009) 8571–8577.
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[16]
2009 | Journal Article | IST-REx-ID: 8477
Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies
C. Amero, P. Schanda, M.A. Durá, I. Ayala, D. Marion, B. Franzetti, B. Brutscher, J. Boisbouvier, Journal of the American Chemical Society 131 (2009) 3448–3449.
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[15]
2009 | Journal Article | IST-REx-ID: 8474
Direct detection of 3hJN' hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy
P. Schanda, M. Huber, R. Verel, M. Ernst, B. Meier, Angewandte Chemie International Edition 48 (2009) 9322–9325.
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[14]
2009 | Journal Article | IST-REx-ID: 8475
Fast-pulsing longitudinal relaxation optimized techniques: Enriching the toolbox of fast biomolecular NMR spectroscopy
P. Schanda, Progress in Nuclear Magnetic Resonance Spectroscopy 55 (2009) 238–265.
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[13]
2008 | Journal Article | IST-REx-ID: 8481
Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge
B. Bersch, A. Favier, P. Schanda, S. van Aelst, T. Vallaeys, J. Covès, M. Mergeay, R. Wattiez, Journal of Molecular Biology 380 (2008) 386–403.
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[12]
2008 | Journal Article | IST-REx-ID: 8480
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
P. Schanda, B. Brutscher, R. Konrat, M. Tollinger, Journal of Molecular Biology 380 (2008) 726–741.
View | DOI
 
[11]
2008 | Journal Article | IST-REx-ID: 8482
Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing 2D NMR with reduced radiofrequency load
T. Kern, P. Schanda, B. Brutscher, Journal of Magnetic Resonance 190 (2008) 333–338.
View | DOI
 
[10]
2007 | Journal Article | IST-REx-ID: 8483
Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy
P. Schanda, V. Forge, B. Brutscher, Proceedings of the National Academy of Sciences 104 (2007) 11257–11262.
View | DOI
 
[9]
2007 | Journal Article | IST-REx-ID: 8487
UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates
M. Gal, P. Schanda, B. Brutscher, L. Frydman, Journal of the American Chemical Society 129 (2007) 1372–1377.
View | DOI
 
[8]
2007 | Journal Article | IST-REx-ID: 8485
Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons
P. Schanda, E. Lescop, M. Falge, R. Sounier, J. Boisbouvier, B. Brutscher, Journal of Biomolecular NMR 38 (2007) 47–55.
View | DOI
 
[7]
2007 | Journal Article | IST-REx-ID: 8486
Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy
E. Lescop, P. Schanda, R. Rasia, B. Brutscher, Journal of the American Chemical Society 129 (2007) 2756–2757.
View | DOI
 
[6]
2007 | Journal Article | IST-REx-ID: 8484
A set of BEST triple-resonance experiments for time-optimized protein resonance assignment
E. Lescop, P. Schanda, B. Brutscher, Journal of Magnetic Resonance 187 (2007) 163–169.
View | DOI
 
[5]
2006 | Journal Article | IST-REx-ID: 8489
HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains
P. Schanda, V. Forge, B. Brutscher, Magnetic Resonance in Chemistry 44 (2006) S177–S184.
View | DOI
 
[4]
2006 | Journal Article | IST-REx-ID: 8488
Speeding up three-dimensional protein NMR experiments to a few minutes
P. Schanda, H. Van Melckebeke, B. Brutscher, Journal of the American Chemical Society 128 (2006) 9042–9043.
View | DOI
 
[3]
2006 | Journal Article | IST-REx-ID: 8490
Hadamard frequency-encoded SOFAST-HMQC for ultrafast two-dimensional protein NMR
P. Schanda, B. Brutscher, Journal of Magnetic Resonance 178 (2006) 334–339.
View | DOI
 
[2]
2005 | Journal Article | IST-REx-ID: 8491
SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds
P. Schanda, Ē. Kupče, B. Brutscher, Journal of Biomolecular NMR 33 (2005) 199–211.
View | DOI
 
[1]
2005 | Journal Article | IST-REx-ID: 8492
Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds
P. Schanda, B. Brutscher, Journal of the American Chemical Society 127 (2005) 8014–8015.
View | DOI
 
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[81]
2023 | Journal Article | IST-REx-ID: 13095 | OA
Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR
L. Troussicot, A. Vallet, M. Molin, B.M. Burmann, P. Schanda, Journal of the American Chemical Society 145 (2023) 10700–10711.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[80]
2023 | Research Data | IST-REx-ID: 12820 | OA
Research data of the publication "Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR"
P. Schanda, (2023).
[Published Version] View | Files available | DOI
 
[79]
2023 | Journal Article | IST-REx-ID: 12114 | OA
Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD
D.F. Gauto, O.O. Lebedenko, L.M. Becker, I. Ayala, R. Lichtenecker, N.R. Skrynnikov, P. Schanda, Journal of Structural Biology: X 7 (2023).
[Published Version] View | Files available | DOI | PubMed | Europe PMC
 
[78]
2023 | Journal Article | IST-REx-ID: 13096 | OA
Structural basis of NINJ1-mediated plasma membrane rupture in cell death
M. Degen, J.C. Santos, K. Pluhackova, G. Cebrero, S. Ramos, G. Jankevicius, E. Hartenian, U. Guillerm, S.A. Mari, B. Kohl, D.J. Müller, P. Schanda, T. Maier, C. Perez, C. Sieben, P. Broz, S. Hiller, Nature 618 (2023) 1065–1071.
[Published Version] View | Files available | DOI | WoS
 
[77]
2023 | Other Publication | IST-REx-ID: 14861 | OA
Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues
L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R. Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Cover Picture: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues, Wiley, 2023.
[Published Version] View | Files available | DOI | Download Published Version (ext.)
 
[76]
2023 | Journal Article | IST-REx-ID: 14835 | OA
Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten
L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R. Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Angewandte Chemie 135 (2023).
[Published Version] View | Files available | DOI
 
[75]
2023 | Book Chapter | IST-REx-ID: 14847 | OA
Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies
I. Sučec, P. Schanda, in:, S. Hiller, M. Liu, L. He (Eds.), Biophysics of Molecular Chaperones, Royal Society of Chemistry, 2023, pp. 136–161.
[Preprint] View | DOI | Download Preprint (ext.)
 
[74]
2023 | Journal Article | IST-REx-ID: 14036 | OA
Protein dynamics detected by magic-angle spinning relaxation dispersion NMR
F. Napoli, L.M. Becker, P. Schanda, Current Opinion in Structural Biology 82 (2023).
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[73]
2023 | Journal Article | IST-REx-ID: 12675 | OA
The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues
L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R. Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Angewandte Chemie International Edition 62 (2023).
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[72]
2023 | Research Data | IST-REx-ID: 12497 | OA
Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues
L.M. Becker, P. Schanda, (2023).
[Published Version] View | Files available | DOI
 
[71]
2022 | Journal Article | IST-REx-ID: 11179 | OA
Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR
D.F. Gauto, P. Macek, D. Malinverni, H. Fraga, M. Paloni, I. Sučec, A. Hessel, J.P. Bustamante, A. Barducci, P. Schanda, Nature Communications 13 (2022).
[Published Version] View | Files available | DOI | WoS
 
[70]
2021 | Journal Article | IST-REx-ID: 10323 | OA
How do chaperones bind (partly) unfolded client proteins?
I. Sučec, B. Bersch, P. Schanda, Frontiers in Molecular Biosciences 8 (2021).
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[69]
2020 | Journal Article | IST-REx-ID: 8402 | OA
The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments
H. Rampelt, I. Sucec, B. Bersch, P. Horten, I. Perschil, J.-C. Martinou, M. van der Laan, N. Wiedemann, P. Schanda, N. Pfanner, BMC Biology 18 (2020).
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[68]
2020 | Preprint | IST-REx-ID: 8404 | OA
Architecture and subunit dynamics of the mitochondrial TIM9·10·12 chaperone
K. Weinhäupl, Y. Wang, A. Hessel, M. Brennich, K. Lindorff-Larsen, P. Schanda, BioRxiv (n.d.).
[Preprint] View | DOI | Download Preprint (ext.)
 
[67]
2020 | Preprint | IST-REx-ID: 8403 | OA
Structural basis of client specificity in mitochondrial membrane-protein chaperones
I. Sučec, Y. Wang, O. Dakhlaoui, K. Weinhäupl, T. Jores, D. Costa, A. Hessel, M. Brennich, D. Rapaport, K. Lindorff-Larsen, B. Bersch, P. Schanda, BioRxiv (n.d.).
[Preprint] View | DOI | Download Preprint (ext.)
 
[66]
2019 | Journal Article | IST-REx-ID: 8405 | OA
Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex
D.F. Gauto, L.F. Estrozi, C.D. Schwieters, G. Effantin, P. Macek, R. Sounier, A.C. Sivertsen, E. Schmidt, R. Kerfah, G. Mas, J.-P. Colletier, P. Güntert, A. Favier, G. Schoehn, P. Schanda, J. Boisbouvier, Nature Communications 10 (2019).
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[65]
2019 | Journal Article | IST-REx-ID: 8406 | OA
Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors
J. Felix, K. Weinhäupl, C. Chipot, F. Dehez, A. Hessel, D.F. Gauto, C. Morlot, O. Abian, I. Gutsche, A. Velazquez-Campoy, P. Schanda, H. Fraga, Science Advances 5 (2019).
[Published Version] View | DOI | Download Published Version (ext.)
 
[64]
2019 | Journal Article | IST-REx-ID: 8413
Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques
P. Rovó, C.A. Smith, D. Gauto, B.L. de Groot, P. Schanda, R. Linser, Journal of the American Chemical Society 141 (2019) 858–869.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[63]
2019 | Journal Article | IST-REx-ID: 8412
Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR
M.D. Shannon, T. Theint, D. Mukhopadhyay, K. Surewicz, W.K. Surewicz, D. Marion, P. Schanda, C.P. Jaroniec, ChemPhysChem 20 (2019) 311–317.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[62]
2019 | Journal Article | IST-REx-ID: 8411
Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR
D. Marion, D.F. Gauto, I. Ayala, K. Giandoreggio-Barranco, P. Schanda, ChemPhysChem 20 (2019) 276–284.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[61]
2019 | Journal Article | IST-REx-ID: 8409
Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency
C. Bougault, I. Ayala, W. Vollmer, J.-P. Simorre, P. Schanda, Journal of Structural Biology 206 (2019) 66–72.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[60]
2019 | Journal Article | IST-REx-ID: 8407
Relaxing with liquids and solids – A perspective on biomolecular dynamics
P. Schanda, Journal of Magnetic Resonance 306 (2019) 180–186.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[59]
2019 | Journal Article | IST-REx-ID: 8410 | OA
NMR for Biological Systems
P. Schanda, E.Y. Chekmenev, ChemPhysChem 20 (2019) 177–177.
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[58]
2019 | Journal Article | IST-REx-ID: 8408
Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR
D.F. Gauto, P. Macek, A. Barducci, H. Fraga, A. Hessel, T. Terauchi, D. Gajan, Y. Miyanoiri, J. Boisbouvier, R. Lichtenecker, M. Kainosho, P. Schanda, Journal of the American Chemical Society 141 (2019) 11183–11195.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[57]
2018 | Journal Article | IST-REx-ID: 8443
How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine
V. Kurauskas, A. Hessel, P. Ma, P. Lunetti, K. Weinhäupl, L. Imbert, B. Brutscher, M.S. King, R. Sounier, V. Dolce, E.R.S. Kunji, L. Capobianco, C. Chipot, F. Dehez, B. Bersch, P. Schanda, The Journal of Physical Chemistry Letters 9 (2018) 933–938.
View | DOI
 
[56]
2018 | Journal Article | IST-REx-ID: 8440
The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis
K. Weinhäupl, M. Brennich, U. Kazmaier, J. Lelievre, L. Ballell, A. Goldberg, P. Schanda, H. Fraga, Journal of Biological Chemistry 293 (2018) 8379–8393.
View | DOI
 
[55]
2018 | Journal Article | IST-REx-ID: 8442
Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies
C. Chipot, F. Dehez, J.R. Schnell, N. Zitzmann, E. Pebay-Peyroula, L.J. Catoire, B. Miroux, E.R.S. Kunji, G. Veglia, T.A. Cross, P. Schanda, Chemical Reviews 118 (2018) 3559–3607.
View | DOI
 
[54]
2018 | Journal Article | IST-REx-ID: 8441
Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals
A. Krushelnitsky, D. Gauto, D.C. Rodriguez Camargo, P. Schanda, K. Saalwächter, Journal of Biomolecular NMR 71 (2018) 53–67.
[Published Version] View | DOI
 
[53]
2018 | Journal Article | IST-REx-ID: 8439
Solid state NMR studies of intact lipopolysaccharide endotoxin
C. Laguri, A. Silipo, A.M. Martorana, P. Schanda, R. Marchetti, A. Polissi, A. Molinaro, J.-P. Simorre, ACS Chemical Biology 13 (2018) 2106–2113.
View | DOI
 
[52]
2018 | Journal Article | IST-REx-ID: 8437
Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle
G. Mas, J.-Y. Guan, E. Crublet, E.C. Debled, C. Moriscot, P. Gans, G. Schoehn, P. Macek, P. Schanda, J. Boisbouvier, Science Advances 4 (2018).
View | DOI
 
[51]
2018 | Journal Article | IST-REx-ID: 8436
Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space
K. Weinhäupl, C. Lindau, A. Hessel, Y. Wang, C. Schütze, T. Jores, L. Melchionda, B. Schönfisch, H. Kalbacher, B. Bersch, D. Rapaport, M. Brennich, K. Lindorff-Larsen, N. Wiedemann, P. Schanda, Cell 175 (2018) 1365–1379.e25.
View | DOI
 
[50]
2018 | Journal Article | IST-REx-ID: 8438
Dynamics and interactions of AAC3 in DPC are not functionally relevant
V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, P. Schanda, Nature Structural & Molecular Biology 25 (2018) 745–747.
View | DOI
 
[49]
2017 | Journal Article | IST-REx-ID: 8446
Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins
H. Fraga, C. Arnaud, D.F. Gauto, M. Audin, V. Kurauskas, P. Macek, C. Krichel, J. Guan, J. Boisbouvier, R. Sprangers, C. Breyton, P. Schanda, ChemPhysChem 18 (2017) 2697–2703.
View | DOI
 
[48]
2017 | Journal Article | IST-REx-ID: 8445
Slow conformational exchange and overall rocking motion in ubiquitin protein crystals
V. Kurauskas, S.A. Izmailov, O.N. Rogacheva, A. Hessel, I. Ayala, J. Woodhouse, A. Shilova, Y. Xue, T. Yuwen, N. Coquelle, J.-P. Colletier, N.R. Skrynnikov, P. Schanda, Nature Communications 8 (2017).
[Published Version] View | DOI
 
[47]
2017 | Journal Article | IST-REx-ID: 8444
Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity
F. Dehez, P. Schanda, M.S. King, E.R.S. Kunji, C. Chipot, Biophysical Journal 113 (2017) 2311–2315.
View | DOI
 
[46]
2017 | Journal Article | IST-REx-ID: 8449
RNA binding and chaperone activity of the E.coli cold-shock protein CspA
E. Rennella, T. Sára, M. Juen, C. Wunderlich, L. Imbert, Z. Solyom, A. Favier, I. Ayala, K. Weinhäupl, P. Schanda, R. Konrat, C. Kreutz, B. Brutscher, Nucleic Acids Research 45 (2017) 4255–4268.
View | DOI
 
[45]
2017 | Journal Article | IST-REx-ID: 8447
Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals
D.F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, P. Schanda, Solid State Nuclear Magnetic Resonance 87 (2017) 86–95.
View | DOI
 
[44]
2017 | Journal Article | IST-REx-ID: 8448
Optimized fast mixing device for real-time NMR applications
R. Franco, A. Favier, P. Schanda, B. Brutscher, Journal of Magnetic Resonance 281 (2017) 125–129.
View | DOI
 
[43]
2017 | Journal Article | IST-REx-ID: 8451
Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native nanodiscs
B. Bersch, J.M. Dörr, A. Hessel, J.A. Killian, P. Schanda, Angewandte Chemie International Edition 56 (2017) 2508–2512.
View | DOI
 
[42]
2017 | Book Chapter | IST-REx-ID: 8450
Methyl-specific isotope labeling strategies for NMR studies of membrane proteins
V. Kurauskas, P. Schanda, R. Sounier, in:, Membrane Protein Structure and Function Characterization, Springer Nature, 2017, pp. 109–123.
View | DOI
 
[41]
2016 | Journal Article | IST-REx-ID: 8455
Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit
V. Kurauskas, E. Crublet, P. Macek, R. Kerfah, D.F. Gauto, J. Boisbouvier, P. Schanda, Chemical Communications 52 (2016) 9558–9561.
View | DOI
 
[40]
2016 | Journal Article | IST-REx-ID: 8453
Cross-correlated relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning R1ρ NMR measurements: Application to protein backbone dynamics measurements
V. Kurauskas, E. Weber, A. Hessel, I. Ayala, D. Marion, P. Schanda, The Journal of Physical Chemistry B 120 (2016) 8905–8913.
View | DOI
 
[39]
2016 | Journal Article | IST-REx-ID: 8452
A ring-shaped conduit connects the mother cell and forespore during sporulation in Bacillus subtilis
C.D.A. Rodrigues, X. Henry, E. Neumann, V. Kurauskas, L. Bellard, Y. Fichou, P. Schanda, G. Schoehn, D.Z. Rudner, C. Morlot, Proceedings of the National Academy of Sciences 113 (2016) 11585–11590.
View | DOI
 
[38]
2016 | Journal Article | IST-REx-ID: 8454
Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules
P. Schanda, M. Ernst, Progress in Nuclear Magnetic Resonance Spectroscopy 96 (2016) 1–46.
View | DOI
 
[37]
2015 | Journal Article | IST-REx-ID: 8456
Observing the overall rocking motion of a protein in a crystal
P. Ma, Y. Xue, N. Coquelle, J.D. Haller, T. Yuwen, I. Ayala, O. Mikhailovskii, D. Willbold, J.-P. Colletier, N.R. Skrynnikov, P. Schanda, Nature Communications 6 (2015).
[Published Version] View | DOI
 
[36]
2015 | Journal Article | IST-REx-ID: 8457
Conformational exchange processes in biological systems: Detection by solid-state NMR
P. Ma, P. Schanda, EMagRes 4 (2015) 699–708.
View | DOI
 
[35]
2014 | Journal Article | IST-REx-ID: 8459
Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data
S. Morin, T.E. Linnet, M. Lescanne, P. Schanda, G.S. Thompson, M. Tollinger, K. Teilum, S. Gagné, D. Marion, C. Griesinger, M. Blackledge, E.J. d’Auvergne, Bioinformatics 30 (2014) 2219–2220.
View | Files available | DOI
 
[34]
2014 | Journal Article | IST-REx-ID: 8458
Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan
P. Schanda, S. Triboulet, C. Laguri, C.M. Bougault, I. Ayala, M. Callon, M. Arthur, J.-P. Simorre, Journal of the American Chemical Society 136 (2014) 17852–17860.
View | DOI
 
[33]
2014 | Journal Article | IST-REx-ID: 8460
Probing transient conformational states of proteins by solid-state R1ρ relaxation-dispersion NMR spectroscopy
P. Ma, J.D. Haller, J. Zajakala, P. Macek, A.C. Sivertsen, D. Willbold, J. Boisbouvier, P. Schanda, Angewandte Chemie International Edition 53 (2014) 4312–4317.
View | DOI
 
[32]
2013 | Journal Article | IST-REx-ID: 8461
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.D. Haller, P. Schanda, Journal of Biomolecular NMR 57 (2013) 263–280.
View | DOI
 
[31]
2013 | Journal Article | IST-REx-ID: 8462
Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure
E. Rennella, T. Cutuil, P. Schanda, I. Ayala, F. Gabel, V. Forge, A. Corazza, G. Esposito, B. Brutscher, Journal of Molecular Biology 425 (2013) 2722–2736.
View | DOI
 
[30]
2012 | Journal Article | IST-REx-ID: 8463
Optimal degree of protonation for 1H detection of aliphatic sites in randomly deuterated proteins as a function of the MAS frequency
S. Asami, K. Szekely, P. Schanda, B.H. Meier, B. Reif, Journal of Biomolecular NMR 54 (2012) 155–168.
View | DOI
 
[29]
2012 | Journal Article | IST-REx-ID: 8465
Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy
M. Tollinger, A.C. Sivertsen, B.H. Meier, M. Ernst, P. Schanda, Journal of the American Chemical Society 134 (2012) 14800–14807.
View | DOI
 
[28]
2012 | Journal Article | IST-REx-ID: 8466
Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate
E. Rennella, T. Cutuil, P. Schanda, I. Ayala, V. Forge, B. Brutscher, Journal of the American Chemical Society 134 (2012) 8066–8069.
View | DOI
 
[27]
2012 | Journal Article | IST-REx-ID: 8467
A supplementary coil for 2H decoupling with commercial HCN MAS probes
M. Huber, O. With, P. Schanda, R. Verel, M. Ernst, B.H. Meier, Journal of Magnetic Resonance 214 (2012) 76–80.
View | DOI
 
[26]
2011 | Journal Article | IST-REx-ID: 8469
Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR
P. Schanda, B.H. Meier, M. Ernst, Journal of Magnetic Resonance 210 (2011) 246–259.
View | DOI
 
[25]
2011 | Journal Article | IST-REx-ID: 8470
A proton-detected 4D solid-state NMR experiment for protein structure determination
M. Huber, S. Hiller, P. Schanda, M. Ernst, A. Böckmann, R. Verel, B.H. Meier, ChemPhysChem 12 (2011) 915–918.
View | DOI
 
[24]
2011 | Journal Article | IST-REx-ID: 8464
Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion
P. Schanda, M. Huber, J. Boisbouvier, B.H. Meier, M. Ernst, Angewandte Chemie International Edition 50 (2011) 11005–11009.
View | Files available | DOI
 
[23]
2011 | Journal Article | IST-REx-ID: 8468
Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins
D. Lalli, P. Schanda, A. Chowdhury, J. Retel, M. Hiller, V.A. Higman, L. Handel, V. Agarwal, B. Reif, B. van Rossum, Ü. Akbey, H. Oschkinat, Journal of Biomolecular NMR 51 (2011) 477–485.
View | DOI
 
[22]
2011 | Journal Article | IST-REx-ID: 8471
Probing water accessibility in HET-s(218–289) amyloid fibrils by solid-state NMR
H. Van Melckebeke, P. Schanda, J. Gath, C. Wasmer, R. Verel, A. Lange, B.H. Meier, A. Böckmann, Journal of Molecular Biology 405 (2011) 765–772.
View | DOI
 
[21]
2010 | Journal Article | IST-REx-ID: 8473
Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR
A. Corazza, E. Rennella, P. Schanda, M.C. Mimmi, T. Cutuil, S. Raimondi, S. Giorgetti, F. Fogolari, P. Viglino, L. Frydman, M. Gal, V. Bellotti, B. Brutscher, G. Esposito, Journal of Biological Chemistry 285 (2010) 5827–5835.
View | DOI
 
[20]
2010 | Journal Article | IST-REx-ID: 8472
Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy
P. Schanda, B.H. Meier, M. Ernst, Journal of the American Chemical Society 132 (2010) 15957–15967.
View | DOI
 
[19]
2009 | Journal Article | IST-REx-ID: 8479
An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates
M. Gal, T. Kern, P. Schanda, L. Frydman, B. Brutscher, Journal of Biomolecular NMR 43 (2009) 1–10.
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[18]
2009 | Journal Article | IST-REx-ID: 8478
Direct observation of the dynamic process underlying allosteric signal transmission
S. Brüschweiler, P. Schanda, K. Kloiber, B. Brutscher, G. Kontaxis, R. Konrat, M. Tollinger, Journal of the American Chemical Society 131 (2009) 3063–3068.
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[17]
2009 | Journal Article | IST-REx-ID: 8476
Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution
J. Farjon, J. Boisbouvier, P. Schanda, A. Pardi, J.-P. Simorre, B. Brutscher, Journal of the American Chemical Society 131 (2009) 8571–8577.
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[16]
2009 | Journal Article | IST-REx-ID: 8477
Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies
C. Amero, P. Schanda, M.A. Durá, I. Ayala, D. Marion, B. Franzetti, B. Brutscher, J. Boisbouvier, Journal of the American Chemical Society 131 (2009) 3448–3449.
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[15]
2009 | Journal Article | IST-REx-ID: 8474
Direct detection of 3hJN' hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy
P. Schanda, M. Huber, R. Verel, M. Ernst, B. Meier, Angewandte Chemie International Edition 48 (2009) 9322–9325.
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[14]
2009 | Journal Article | IST-REx-ID: 8475
Fast-pulsing longitudinal relaxation optimized techniques: Enriching the toolbox of fast biomolecular NMR spectroscopy
P. Schanda, Progress in Nuclear Magnetic Resonance Spectroscopy 55 (2009) 238–265.
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[13]
2008 | Journal Article | IST-REx-ID: 8481
Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge
B. Bersch, A. Favier, P. Schanda, S. van Aelst, T. Vallaeys, J. Covès, M. Mergeay, R. Wattiez, Journal of Molecular Biology 380 (2008) 386–403.
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[12]
2008 | Journal Article | IST-REx-ID: 8480
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
P. Schanda, B. Brutscher, R. Konrat, M. Tollinger, Journal of Molecular Biology 380 (2008) 726–741.
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[11]
2008 | Journal Article | IST-REx-ID: 8482
Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing 2D NMR with reduced radiofrequency load
T. Kern, P. Schanda, B. Brutscher, Journal of Magnetic Resonance 190 (2008) 333–338.
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[10]
2007 | Journal Article | IST-REx-ID: 8483
Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy
P. Schanda, V. Forge, B. Brutscher, Proceedings of the National Academy of Sciences 104 (2007) 11257–11262.
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[9]
2007 | Journal Article | IST-REx-ID: 8487
UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates
M. Gal, P. Schanda, B. Brutscher, L. Frydman, Journal of the American Chemical Society 129 (2007) 1372–1377.
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[8]
2007 | Journal Article | IST-REx-ID: 8485
Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons
P. Schanda, E. Lescop, M. Falge, R. Sounier, J. Boisbouvier, B. Brutscher, Journal of Biomolecular NMR 38 (2007) 47–55.
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[7]
2007 | Journal Article | IST-REx-ID: 8486
Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy
E. Lescop, P. Schanda, R. Rasia, B. Brutscher, Journal of the American Chemical Society 129 (2007) 2756–2757.
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[6]
2007 | Journal Article | IST-REx-ID: 8484
A set of BEST triple-resonance experiments for time-optimized protein resonance assignment
E. Lescop, P. Schanda, B. Brutscher, Journal of Magnetic Resonance 187 (2007) 163–169.
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[5]
2006 | Journal Article | IST-REx-ID: 8489
HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains
P. Schanda, V. Forge, B. Brutscher, Magnetic Resonance in Chemistry 44 (2006) S177–S184.
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[4]
2006 | Journal Article | IST-REx-ID: 8488
Speeding up three-dimensional protein NMR experiments to a few minutes
P. Schanda, H. Van Melckebeke, B. Brutscher, Journal of the American Chemical Society 128 (2006) 9042–9043.
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[3]
2006 | Journal Article | IST-REx-ID: 8490
Hadamard frequency-encoded SOFAST-HMQC for ultrafast two-dimensional protein NMR
P. Schanda, B. Brutscher, Journal of Magnetic Resonance 178 (2006) 334–339.
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[2]
2005 | Journal Article | IST-REx-ID: 8491
SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds
P. Schanda, Ē. Kupče, B. Brutscher, Journal of Biomolecular NMR 33 (2005) 199–211.
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[1]
2005 | Journal Article | IST-REx-ID: 8492
Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds
P. Schanda, B. Brutscher, Journal of the American Chemical Society 127 (2005) 8014–8015.
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