Paul Schanda

Schanda Group

81 Publications

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[81]
2023 | Journal Article | IST-REx-ID: 13095 | OA
Troussicot L, Vallet A, Molin M, Burmann BM, Schanda P. Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR. Journal of the American Chemical Society. 2023;145(19):10700–10711. doi:10.1021/jacs.3c01200
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[80]
2023 | Research Data | IST-REx-ID: 12820 | OA
Schanda P. Research data of the publication “Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR.” 2023. doi:10.15479/AT:ISTA:12820
[Published Version] View | Files available | DOI
 
[79]
2023 | Journal Article | IST-REx-ID: 12114 | OA
Gauto DF, Lebedenko OO, Becker LM, et al. Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD. Journal of Structural Biology: X. 2023;7. doi:10.1016/j.yjsbx.2022.100079
[Published Version] View | Files available | DOI | PubMed | Europe PMC
 
[78]
2023 | Journal Article | IST-REx-ID: 13096 | OA
Degen M, Santos JC, Pluhackova K, et al. Structural basis of NINJ1-mediated plasma membrane rupture in cell death. Nature. 2023;618:1065-1071. doi:10.1038/s41586-023-05991-z
[Published Version] View | Files available | DOI | WoS
 
[77]
2023 | Other Publication | IST-REx-ID: 14861 | OA
Becker LM, Berbon M, Vallet A, et al. Cover Picture: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues. Vol 62. Wiley; 2023. doi:10.1002/anie.202304138
[Published Version] View | Files available | DOI | Download Published Version (ext.)
 
[76]
2023 | Journal Article | IST-REx-ID: 14835 | OA
Becker LM, Berbon M, Vallet A, et al. Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten. Angewandte Chemie. 2023;135(19). doi:10.1002/ange.202219314
[Published Version] View | Files available | DOI
 
[75]
2023 | Book Chapter | IST-REx-ID: 14847 | OA
Sučec I, Schanda P. Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies. In: Hiller S, Liu M, He L, eds. Biophysics of Molecular Chaperones. Vol 29. Royal Society of Chemistry; 2023:136-161. doi:10.1039/bk9781839165986-00136
[Preprint] View | DOI | Download Preprint (ext.)
 
[74]
2023 | Journal Article | IST-REx-ID: 14036 | OA
Napoli F, Becker LM, Schanda P. Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. Current Opinion in Structural Biology. 2023;82(10). doi:10.1016/j.sbi.2023.102660
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[73]
2023 | Journal Article | IST-REx-ID: 12675 | OA
Becker LM, Berbon M, Vallet A, et al. The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues. Angewandte Chemie International Edition. 2023;62(19). doi:10.1002/anie.202219314
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[72]
2023 | Research Data | IST-REx-ID: 12497 | OA
Becker LM, Schanda P. Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues. 2023. doi:10.15479/AT:ISTA:12497
[Published Version] View | Files available | DOI
 
[71]
2022 | Journal Article | IST-REx-ID: 11179 | OA
Gauto DF, Macek P, Malinverni D, et al. Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR. Nature Communications. 2022;13. doi:10.1038/s41467-022-29423-0
[Published Version] View | Files available | DOI | WoS
 
[70]
2021 | Journal Article | IST-REx-ID: 10323 | OA
Sučec I, Bersch B, Schanda P. How do chaperones bind (partly) unfolded client proteins? Frontiers in Molecular Biosciences. 2021;8. doi:10.3389/fmolb.2021.762005
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[69]
2020 | Journal Article | IST-REx-ID: 8402 | OA
Rampelt H, Sucec I, Bersch B, et al. The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments. BMC Biology. 2020;18. doi:10.1186/s12915-019-0733-6
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[68]
2020 | Preprint | IST-REx-ID: 8404 | OA
Weinhäupl K, Wang Y, Hessel A, Brennich M, Lindorff-Larsen K, Schanda P. Architecture and subunit dynamics of the mitochondrial TIM9·10·12 chaperone. bioRxiv. doi:10.1101/2020.03.13.990150
[Preprint] View | DOI | Download Preprint (ext.)
 
[67]
2020 | Preprint | IST-REx-ID: 8403 | OA
Sučec I, Wang Y, Dakhlaoui O, et al. Structural basis of client specificity in mitochondrial membrane-protein chaperones. bioRxiv. doi:10.1101/2020.06.08.140772
[Preprint] View | DOI | Download Preprint (ext.)
 
[66]
2019 | Journal Article | IST-REx-ID: 8405 | OA
Gauto DF, Estrozi LF, Schwieters CD, et al. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications. 2019;10. doi:10.1038/s41467-019-10490-9
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[65]
2019 | Journal Article | IST-REx-ID: 8406 | OA
Felix J, Weinhäupl K, Chipot C, et al. Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors. Science Advances. 2019;5(9). doi:10.1126/sciadv.aaw3818
[Published Version] View | DOI | Download Published Version (ext.)
 
[64]
2019 | Journal Article | IST-REx-ID: 8413
Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques. Journal of the American Chemical Society. 2019;141(2):858-869. doi:10.1021/jacs.8b09258
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[63]
2019 | Journal Article | IST-REx-ID: 8412
Shannon MD, Theint T, Mukhopadhyay D, et al. Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR. ChemPhysChem. 2019;20(2):311-317. doi:10.1002/cphc.201800779
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[62]
2019 | Journal Article | IST-REx-ID: 8411
Marion D, Gauto DF, Ayala I, Giandoreggio-Barranco K, Schanda P. Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR. ChemPhysChem. 2019;20(2):276-284. doi:10.1002/cphc.201800935
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[61]
2019 | Journal Article | IST-REx-ID: 8409
Bougault C, Ayala I, Vollmer W, Simorre J-P, Schanda P. Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency. Journal of Structural Biology. 2019;206(1):66-72. doi:10.1016/j.jsb.2018.07.009
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[60]
2019 | Journal Article | IST-REx-ID: 8407
Schanda P. Relaxing with liquids and solids – A perspective on biomolecular dynamics. Journal of Magnetic Resonance. 2019;306:180-186. doi:10.1016/j.jmr.2019.07.025
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[59]
2019 | Journal Article | IST-REx-ID: 8410 | OA
Schanda P, Chekmenev EY. NMR for Biological Systems. ChemPhysChem. 2019;20(2):177-177. doi:10.1002/cphc.201801100
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[58]
2019 | Journal Article | IST-REx-ID: 8408
Gauto DF, Macek P, Barducci A, 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. Journal of the American Chemical Society. 2019;141(28):11183-11195. doi:10.1021/jacs.9b04219
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[57]
2018 | Journal Article | IST-REx-ID: 8443
Kurauskas V, Hessel A, Ma P, et al. How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine. The Journal of Physical Chemistry Letters. 2018;9(5):933-938. doi:10.1021/acs.jpclett.8b00269
View | DOI
 
[56]
2018 | Journal Article | IST-REx-ID: 8440
Weinhäupl K, Brennich M, Kazmaier U, et al. The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. Journal of Biological Chemistry. 2018;293(22):8379-8393. doi:10.1074/jbc.ra118.002251
View | DOI
 
[55]
2018 | Journal Article | IST-REx-ID: 8442
Chipot C, Dehez F, Schnell JR, et al. Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. Chemical Reviews. 2018;118(7):3559-3607. doi:10.1021/acs.chemrev.7b00570
View | DOI
 
[54]
2018 | Journal Article | IST-REx-ID: 8441
Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K. Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals. Journal of Biomolecular NMR. 2018;71(1):53-67. doi:10.1007/s10858-018-0191-4
[Published Version] View | DOI
 
[53]
2018 | Journal Article | IST-REx-ID: 8439
Laguri C, Silipo A, Martorana AM, et al. Solid state NMR studies of intact lipopolysaccharide endotoxin. ACS Chemical Biology. 2018;13(8):2106-2113. doi:10.1021/acschembio.8b00271
View | DOI
 
[52]
2018 | Journal Article | IST-REx-ID: 8437
Mas G, Guan J-Y, Crublet E, et al. Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle. Science Advances. 2018;4(9). doi:10.1126/sciadv.aau4196
View | DOI
 
[51]
2018 | Journal Article | IST-REx-ID: 8436
Weinhäupl K, Lindau C, Hessel A, et al. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell. 2018;175(5):1365-1379.e25. doi:10.1016/j.cell.2018.10.039
View | DOI
 
[50]
2018 | Journal Article | IST-REx-ID: 8438
Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. Dynamics and interactions of AAC3 in DPC are not functionally relevant. Nature Structural & Molecular Biology. 2018;25(9):745-747. doi:10.1038/s41594-018-0127-4
View | DOI
 
[49]
2017 | Journal Article | IST-REx-ID: 8446
Fraga H, Arnaud C, Gauto DF, et al. Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. ChemPhysChem. 2017;18(19):2697-2703. doi:10.1002/cphc.201700572
View | DOI
 
[48]
2017 | Journal Article | IST-REx-ID: 8445
Kurauskas V, Izmailov SA, Rogacheva ON, et al. Slow conformational exchange and overall rocking motion in ubiquitin protein crystals. Nature Communications. 2017;8. doi:10.1038/s41467-017-00165-8
[Published Version] View | DOI
 
[47]
2017 | Journal Article | IST-REx-ID: 8444
Dehez F, Schanda P, King MS, Kunji ERS, Chipot C. Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity. Biophysical Journal. 2017;113(11):2311-2315. doi:10.1016/j.bpj.2017.09.019
View | DOI
 
[46]
2017 | Journal Article | IST-REx-ID: 8449
Rennella E, Sára T, Juen M, et al. RNA binding and chaperone activity of the E.coli cold-shock protein CspA. Nucleic Acids Research. 2017;45(7):4255-4268. doi:10.1093/nar/gkx044
View | DOI
 
[45]
2017 | Journal Article | IST-REx-ID: 8447
Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance. 2017;87(10):86-95. doi:10.1016/j.ssnmr.2017.04.002
View | DOI
 
[44]
2017 | Journal Article | IST-REx-ID: 8448
Franco R, Favier A, Schanda P, Brutscher B. Optimized fast mixing device for real-time NMR applications. Journal of Magnetic Resonance. 2017;281(8):125-129. doi:10.1016/j.jmr.2017.05.016
View | DOI
 
[43]
2017 | Journal Article | IST-REx-ID: 8451
Bersch B, Dörr JM, Hessel A, Killian JA, Schanda P. Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native nanodiscs. Angewandte Chemie International Edition. 2017;56(9):2508-2512. doi:10.1002/anie.201610441
View | DOI
 
[42]
2017 | Book Chapter | IST-REx-ID: 8450
Kurauskas V, Schanda P, Sounier R. Methyl-specific isotope labeling strategies for NMR studies of membrane proteins. In: Membrane Protein Structure and Function Characterization. Vol 1635. Springer Nature; 2017:109-123. doi:10.1007/978-1-4939-7151-0_6
View | DOI
 
[41]
2016 | Journal Article | IST-REx-ID: 8455
Kurauskas V, Crublet E, Macek P, et al. Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit. Chemical Communications. 2016;52(61):9558-9561. doi:10.1039/c6cc04484k
View | DOI
 
[40]
2016 | Journal Article | IST-REx-ID: 8453
Kurauskas V, Weber E, Hessel A, Ayala I, Marion D, Schanda P. Cross-correlated relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning R1ρ NMR measurements: Application to protein backbone dynamics measurements. The Journal of Physical Chemistry B. 2016;120(34):8905-8913. doi:10.1021/acs.jpcb.6b06129
View | DOI
 
[39]
2016 | Journal Article | IST-REx-ID: 8452
Rodrigues CDA, Henry X, Neumann E, et al. A ring-shaped conduit connects the mother cell and forespore during sporulation in Bacillus subtilis. Proceedings of the National Academy of Sciences. 2016;113(41):11585-11590. doi:10.1073/pnas.1609604113
View | DOI
 
[38]
2016 | Journal Article | IST-REx-ID: 8454
Schanda P, Ernst M. Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules. Progress in Nuclear Magnetic Resonance Spectroscopy. 2016;96(8):1-46. doi:10.1016/j.pnmrs.2016.02.001
View | DOI
 
[37]
2015 | Journal Article | IST-REx-ID: 8456
Ma P, Xue Y, Coquelle N, et al. Observing the overall rocking motion of a protein in a crystal. Nature Communications. 2015;6. doi:10.1038/ncomms9361
[Published Version] View | DOI
 
[36]
2015 | Journal Article | IST-REx-ID: 8457
Ma P, Schanda P. Conformational exchange processes in biological systems: Detection by solid-state NMR. eMagRes. 2015;4(3):699-708. doi:10.1002/9780470034590.emrstm1418
View | DOI
 
[35]
2014 | Journal Article | IST-REx-ID: 8459
Morin S, Linnet TE, Lescanne M, et al. Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. Bioinformatics. 2014;30(15):2219-2220. doi:10.1093/bioinformatics/btu166
View | Files available | DOI
 
[34]
2014 | Journal Article | IST-REx-ID: 8458
Schanda P, Triboulet S, Laguri C, et al. Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan. Journal of the American Chemical Society. 2014;136(51):17852-17860. doi:10.1021/ja5105987
View | DOI
 
[33]
2014 | Journal Article | IST-REx-ID: 8460
Ma P, Haller JD, Zajakala J, et al. Probing transient conformational states of proteins by solid-state R1ρ relaxation-dispersion NMR spectroscopy. Angewandte Chemie International Edition. 2014;53(17):4312-4317. doi:10.1002/anie.201311275
View | DOI
 
[32]
2013 | Journal Article | IST-REx-ID: 8461
Haller JD, Schanda P. Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin. Journal of Biomolecular NMR. 2013;57(3):263-280. doi:10.1007/s10858-013-9787-x
View | DOI
 
[31]
2013 | Journal Article | IST-REx-ID: 8462
Rennella E, Cutuil T, Schanda P, et al. Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure. Journal of Molecular Biology. 2013;425(15):2722-2736. doi:10.1016/j.jmb.2013.04.028
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[30]
2012 | Journal Article | IST-REx-ID: 8463
Asami S, Szekely K, Schanda P, Meier BH, Reif B. Optimal degree of protonation for 1H detection of aliphatic sites in randomly deuterated proteins as a function of the MAS frequency. Journal of Biomolecular NMR. 2012;54(2):155-168. doi:10.1007/s10858-012-9659-9
View | DOI
 
[29]
2012 | Journal Article | IST-REx-ID: 8465
Tollinger M, Sivertsen AC, Meier BH, Ernst M, Schanda P. Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy. Journal of the American Chemical Society. 2012;134(36):14800-14807. doi:10.1021/ja303591y
View | DOI
 
[28]
2012 | Journal Article | IST-REx-ID: 8466
Rennella E, Cutuil T, Schanda P, Ayala I, Forge V, Brutscher B. Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate. Journal of the American Chemical Society. 2012;134(19):8066-8069. doi:10.1021/ja302598j
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[27]
2012 | Journal Article | IST-REx-ID: 8467
Huber M, With O, Schanda P, Verel R, Ernst M, Meier BH. A supplementary coil for 2H decoupling with commercial HCN MAS probes. Journal of Magnetic Resonance. 2012;214:76-80. doi:10.1016/j.jmr.2011.10.010
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[26]
2011 | Journal Article | IST-REx-ID: 8469
Schanda P, Meier BH, Ernst M. Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR. Journal of Magnetic Resonance. 2011;210(2):246-259. doi:10.1016/j.jmr.2011.03.015
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[25]
2011 | Journal Article | IST-REx-ID: 8470
Huber M, Hiller S, Schanda P, et al. A proton-detected 4D solid-state NMR experiment for protein structure determination. ChemPhysChem. 2011;12(5):915-918. doi:10.1002/cphc.201100062
View | DOI
 
[24]
2011 | Journal Article | IST-REx-ID: 8464
Schanda P, Huber M, Boisbouvier J, Meier BH, Ernst M. Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion. Angewandte Chemie International Edition. 2011;50(46):11005-11009. doi:10.1002/anie.201103944
View | Files available | DOI
 
[23]
2011 | Journal Article | IST-REx-ID: 8468
Lalli D, Schanda P, Chowdhury A, et al. Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins. Journal of Biomolecular NMR. 2011;51(4):477-485. doi:10.1007/s10858-011-9578-1
View | DOI
 
[22]
2011 | Journal Article | IST-REx-ID: 8471
Van Melckebeke H, Schanda P, Gath J, et al. Probing water accessibility in HET-s(218–289) amyloid fibrils by solid-state NMR. Journal of Molecular Biology. 2011;405(3):765-772. doi:10.1016/j.jmb.2010.11.004
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[21]
2010 | Journal Article | IST-REx-ID: 8473
Corazza A, Rennella E, Schanda P, et al. Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR. Journal of Biological Chemistry. 2010;285(8):5827-5835. doi:10.1074/jbc.m109.061168
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[20]
2010 | Journal Article | IST-REx-ID: 8472
Schanda P, Meier BH, Ernst M. Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy. Journal of the American Chemical Society. 2010;132(45):15957-15967. doi:10.1021/ja100726a
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[19]
2009 | Journal Article | IST-REx-ID: 8479
Gal M, Kern T, Schanda P, Frydman L, Brutscher B. An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates. Journal of Biomolecular NMR. 2009;43:1-10. doi:10.1007/s10858-008-9284-9
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[18]
2009 | Journal Article | IST-REx-ID: 8478
Brüschweiler S, Schanda P, Kloiber K, et al. Direct observation of the dynamic process underlying allosteric signal transmission. Journal of the American Chemical Society. 2009;131(8):3063-3068. doi:10.1021/ja809947w
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[17]
2009 | Journal Article | IST-REx-ID: 8476
Farjon J, Boisbouvier J, Schanda P, Pardi A, Simorre J-P, Brutscher B. Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution. Journal of the American Chemical Society. 2009;131(24):8571-8577. doi:10.1021/ja901633y
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[16]
2009 | Journal Article | IST-REx-ID: 8477
Amero C, Schanda P, Durá MA, et al. Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies. Journal of the American Chemical Society. 2009;131(10):3448-3449. doi:10.1021/ja809880p
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[15]
2009 | Journal Article | IST-REx-ID: 8474
Schanda P, Huber M, Verel R, Ernst M, Meier B. Direct detection of 3hJN’ hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy. Angewandte Chemie International Edition. 2009;48(49):9322-9325. doi:10.1002/anie.200904411
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[14]
2009 | Journal Article | IST-REx-ID: 8475
Schanda P. Fast-pulsing longitudinal relaxation optimized techniques: Enriching the toolbox of fast biomolecular NMR spectroscopy. Progress in Nuclear Magnetic Resonance Spectroscopy. 2009;55(3):238-265. doi:10.1016/j.pnmrs.2009.05.002
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[13]
2008 | Journal Article | IST-REx-ID: 8481
Bersch B, Favier A, Schanda P, et al. Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge. Journal of Molecular Biology. 2008;380(2):386-403. doi:10.1016/j.jmb.2008.05.017
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[12]
2008 | Journal Article | IST-REx-ID: 8480
Schanda P, Brutscher B, Konrat R, Tollinger M. 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. Journal of Molecular Biology. 2008;380(4):726-741. doi:10.1016/j.jmb.2008.05.040
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[11]
2008 | Journal Article | IST-REx-ID: 8482
Kern T, Schanda P, Brutscher B. Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing 2D NMR with reduced radiofrequency load. Journal of Magnetic Resonance. 2008;190(2):333-338. doi:10.1016/j.jmr.2007.11.015
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[10]
2007 | Journal Article | IST-REx-ID: 8483
Schanda P, Forge V, Brutscher B. Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy. Proceedings of the National Academy of Sciences. 2007;104(27):11257-11262. doi:10.1073/pnas.0702069104
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[9]
2007 | Journal Article | IST-REx-ID: 8487
Gal M, Schanda P, Brutscher B, Frydman L. UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates. Journal of the American Chemical Society. 2007;129(5):1372-1377. doi:10.1021/ja066915g
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[8]
2007 | Journal Article | IST-REx-ID: 8485
Schanda P, Lescop E, Falge M, Sounier R, Boisbouvier J, Brutscher B. Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons. Journal of Biomolecular NMR. 2007;38:47-55. doi:10.1007/s10858-006-9138-2
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[7]
2007 | Journal Article | IST-REx-ID: 8486
Lescop E, Schanda P, Rasia R, Brutscher B. Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy. Journal of the American Chemical Society. 2007;129(10):2756-2757. doi:10.1021/ja068949u
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[6]
2007 | Journal Article | IST-REx-ID: 8484
Lescop E, Schanda P, Brutscher B. A set of BEST triple-resonance experiments for time-optimized protein resonance assignment. Journal of Magnetic Resonance. 2007;187(1):163-169. doi:10.1016/j.jmr.2007.04.002
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[5]
2006 | Journal Article | IST-REx-ID: 8489
Schanda P, Forge V, Brutscher B. HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains. Magnetic Resonance in Chemistry. 2006;44(S1):S177-S184. doi:10.1002/mrc.1825
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[4]
2006 | Journal Article | IST-REx-ID: 8488
Schanda P, Van Melckebeke H, Brutscher B. Speeding up three-dimensional protein NMR experiments to a few minutes. Journal of the American Chemical Society. 2006;128(28):9042-9043. doi:10.1021/ja062025p
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[3]
2006 | Journal Article | IST-REx-ID: 8490
Schanda P, Brutscher B. Hadamard frequency-encoded SOFAST-HMQC for ultrafast two-dimensional protein NMR. Journal of Magnetic Resonance. 2006;178(2):334-339. doi:10.1016/j.jmr.2005.10.007
View | DOI
 
[2]
2005 | Journal Article | IST-REx-ID: 8491
Schanda P, Kupče Ē, Brutscher B. SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds. Journal of Biomolecular NMR. 2005;33(4):199-211. doi:10.1007/s10858-005-4425-x
View | DOI
 
[1]
2005 | Journal Article | IST-REx-ID: 8492
Schanda P, Brutscher B. Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. Journal of the American Chemical Society. 2005;127(22):8014-8015. doi:10.1021/ja051306e
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[81]
2023 | Journal Article | IST-REx-ID: 13095 | OA
Troussicot L, Vallet A, Molin M, Burmann BM, Schanda P. Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR. Journal of the American Chemical Society. 2023;145(19):10700–10711. doi:10.1021/jacs.3c01200
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[80]
2023 | Research Data | IST-REx-ID: 12820 | OA
Schanda P. Research data of the publication “Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR.” 2023. doi:10.15479/AT:ISTA:12820
[Published Version] View | Files available | DOI
 
[79]
2023 | Journal Article | IST-REx-ID: 12114 | OA
Gauto DF, Lebedenko OO, Becker LM, et al. Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD. Journal of Structural Biology: X. 2023;7. doi:10.1016/j.yjsbx.2022.100079
[Published Version] View | Files available | DOI | PubMed | Europe PMC
 
[78]
2023 | Journal Article | IST-REx-ID: 13096 | OA
Degen M, Santos JC, Pluhackova K, et al. Structural basis of NINJ1-mediated plasma membrane rupture in cell death. Nature. 2023;618:1065-1071. doi:10.1038/s41586-023-05991-z
[Published Version] View | Files available | DOI | WoS
 
[77]
2023 | Other Publication | IST-REx-ID: 14861 | OA
Becker LM, Berbon M, Vallet A, et al. Cover Picture: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues. Vol 62. Wiley; 2023. doi:10.1002/anie.202304138
[Published Version] View | Files available | DOI | Download Published Version (ext.)
 
[76]
2023 | Journal Article | IST-REx-ID: 14835 | OA
Becker LM, Berbon M, Vallet A, et al. Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten. Angewandte Chemie. 2023;135(19). doi:10.1002/ange.202219314
[Published Version] View | Files available | DOI
 
[75]
2023 | Book Chapter | IST-REx-ID: 14847 | OA
Sučec I, Schanda P. Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies. In: Hiller S, Liu M, He L, eds. Biophysics of Molecular Chaperones. Vol 29. Royal Society of Chemistry; 2023:136-161. doi:10.1039/bk9781839165986-00136
[Preprint] View | DOI | Download Preprint (ext.)
 
[74]
2023 | Journal Article | IST-REx-ID: 14036 | OA
Napoli F, Becker LM, Schanda P. Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. Current Opinion in Structural Biology. 2023;82(10). doi:10.1016/j.sbi.2023.102660
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[73]
2023 | Journal Article | IST-REx-ID: 12675 | OA
Becker LM, Berbon M, Vallet A, et al. The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues. Angewandte Chemie International Edition. 2023;62(19). doi:10.1002/anie.202219314
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[72]
2023 | Research Data | IST-REx-ID: 12497 | OA
Becker LM, Schanda P. Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues. 2023. doi:10.15479/AT:ISTA:12497
[Published Version] View | Files available | DOI
 
[71]
2022 | Journal Article | IST-REx-ID: 11179 | OA
Gauto DF, Macek P, Malinverni D, et al. Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR. Nature Communications. 2022;13. doi:10.1038/s41467-022-29423-0
[Published Version] View | Files available | DOI | WoS
 
[70]
2021 | Journal Article | IST-REx-ID: 10323 | OA
Sučec I, Bersch B, Schanda P. How do chaperones bind (partly) unfolded client proteins? Frontiers in Molecular Biosciences. 2021;8. doi:10.3389/fmolb.2021.762005
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[69]
2020 | Journal Article | IST-REx-ID: 8402 | OA
Rampelt H, Sucec I, Bersch B, et al. The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments. BMC Biology. 2020;18. doi:10.1186/s12915-019-0733-6
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[68]
2020 | Preprint | IST-REx-ID: 8404 | OA
Weinhäupl K, Wang Y, Hessel A, Brennich M, Lindorff-Larsen K, Schanda P. Architecture and subunit dynamics of the mitochondrial TIM9·10·12 chaperone. bioRxiv. doi:10.1101/2020.03.13.990150
[Preprint] View | DOI | Download Preprint (ext.)
 
[67]
2020 | Preprint | IST-REx-ID: 8403 | OA
Sučec I, Wang Y, Dakhlaoui O, et al. Structural basis of client specificity in mitochondrial membrane-protein chaperones. bioRxiv. doi:10.1101/2020.06.08.140772
[Preprint] View | DOI | Download Preprint (ext.)
 
[66]
2019 | Journal Article | IST-REx-ID: 8405 | OA
Gauto DF, Estrozi LF, Schwieters CD, et al. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications. 2019;10. doi:10.1038/s41467-019-10490-9
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[65]
2019 | Journal Article | IST-REx-ID: 8406 | OA
Felix J, Weinhäupl K, Chipot C, et al. Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors. Science Advances. 2019;5(9). doi:10.1126/sciadv.aaw3818
[Published Version] View | DOI | Download Published Version (ext.)
 
[64]
2019 | Journal Article | IST-REx-ID: 8413
Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques. Journal of the American Chemical Society. 2019;141(2):858-869. doi:10.1021/jacs.8b09258
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[63]
2019 | Journal Article | IST-REx-ID: 8412
Shannon MD, Theint T, Mukhopadhyay D, et al. Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR. ChemPhysChem. 2019;20(2):311-317. doi:10.1002/cphc.201800779
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[62]
2019 | Journal Article | IST-REx-ID: 8411
Marion D, Gauto DF, Ayala I, Giandoreggio-Barranco K, Schanda P. Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR. ChemPhysChem. 2019;20(2):276-284. doi:10.1002/cphc.201800935
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[61]
2019 | Journal Article | IST-REx-ID: 8409
Bougault C, Ayala I, Vollmer W, Simorre J-P, Schanda P. Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency. Journal of Structural Biology. 2019;206(1):66-72. doi:10.1016/j.jsb.2018.07.009
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[60]
2019 | Journal Article | IST-REx-ID: 8407
Schanda P. Relaxing with liquids and solids – A perspective on biomolecular dynamics. Journal of Magnetic Resonance. 2019;306:180-186. doi:10.1016/j.jmr.2019.07.025
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[59]
2019 | Journal Article | IST-REx-ID: 8410 | OA
Schanda P, Chekmenev EY. NMR for Biological Systems. ChemPhysChem. 2019;20(2):177-177. doi:10.1002/cphc.201801100
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[58]
2019 | Journal Article | IST-REx-ID: 8408
Gauto DF, Macek P, Barducci A, 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. Journal of the American Chemical Society. 2019;141(28):11183-11195. doi:10.1021/jacs.9b04219
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[57]
2018 | Journal Article | IST-REx-ID: 8443
Kurauskas V, Hessel A, Ma P, et al. How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine. The Journal of Physical Chemistry Letters. 2018;9(5):933-938. doi:10.1021/acs.jpclett.8b00269
View | DOI
 
[56]
2018 | Journal Article | IST-REx-ID: 8440
Weinhäupl K, Brennich M, Kazmaier U, et al. The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. Journal of Biological Chemistry. 2018;293(22):8379-8393. doi:10.1074/jbc.ra118.002251
View | DOI
 
[55]
2018 | Journal Article | IST-REx-ID: 8442
Chipot C, Dehez F, Schnell JR, et al. Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. Chemical Reviews. 2018;118(7):3559-3607. doi:10.1021/acs.chemrev.7b00570
View | DOI
 
[54]
2018 | Journal Article | IST-REx-ID: 8441
Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K. Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals. Journal of Biomolecular NMR. 2018;71(1):53-67. doi:10.1007/s10858-018-0191-4
[Published Version] View | DOI
 
[53]
2018 | Journal Article | IST-REx-ID: 8439
Laguri C, Silipo A, Martorana AM, et al. Solid state NMR studies of intact lipopolysaccharide endotoxin. ACS Chemical Biology. 2018;13(8):2106-2113. doi:10.1021/acschembio.8b00271
View | DOI
 
[52]
2018 | Journal Article | IST-REx-ID: 8437
Mas G, Guan J-Y, Crublet E, et al. Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle. Science Advances. 2018;4(9). doi:10.1126/sciadv.aau4196
View | DOI
 
[51]
2018 | Journal Article | IST-REx-ID: 8436
Weinhäupl K, Lindau C, Hessel A, et al. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell. 2018;175(5):1365-1379.e25. doi:10.1016/j.cell.2018.10.039
View | DOI
 
[50]
2018 | Journal Article | IST-REx-ID: 8438
Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. Dynamics and interactions of AAC3 in DPC are not functionally relevant. Nature Structural & Molecular Biology. 2018;25(9):745-747. doi:10.1038/s41594-018-0127-4
View | DOI
 
[49]
2017 | Journal Article | IST-REx-ID: 8446
Fraga H, Arnaud C, Gauto DF, et al. Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. ChemPhysChem. 2017;18(19):2697-2703. doi:10.1002/cphc.201700572
View | DOI
 
[48]
2017 | Journal Article | IST-REx-ID: 8445
Kurauskas V, Izmailov SA, Rogacheva ON, et al. Slow conformational exchange and overall rocking motion in ubiquitin protein crystals. Nature Communications. 2017;8. doi:10.1038/s41467-017-00165-8
[Published Version] View | DOI
 
[47]
2017 | Journal Article | IST-REx-ID: 8444
Dehez F, Schanda P, King MS, Kunji ERS, Chipot C. Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity. Biophysical Journal. 2017;113(11):2311-2315. doi:10.1016/j.bpj.2017.09.019
View | DOI
 
[46]
2017 | Journal Article | IST-REx-ID: 8449
Rennella E, Sára T, Juen M, et al. RNA binding and chaperone activity of the E.coli cold-shock protein CspA. Nucleic Acids Research. 2017;45(7):4255-4268. doi:10.1093/nar/gkx044
View | DOI
 
[45]
2017 | Journal Article | IST-REx-ID: 8447
Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance. 2017;87(10):86-95. doi:10.1016/j.ssnmr.2017.04.002
View | DOI
 
[44]
2017 | Journal Article | IST-REx-ID: 8448
Franco R, Favier A, Schanda P, Brutscher B. Optimized fast mixing device for real-time NMR applications. Journal of Magnetic Resonance. 2017;281(8):125-129. doi:10.1016/j.jmr.2017.05.016
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[43]
2017 | Journal Article | IST-REx-ID: 8451
Bersch B, Dörr JM, Hessel A, Killian JA, Schanda P. Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native nanodiscs. Angewandte Chemie International Edition. 2017;56(9):2508-2512. doi:10.1002/anie.201610441
View | DOI
 
[42]
2017 | Book Chapter | IST-REx-ID: 8450
Kurauskas V, Schanda P, Sounier R. Methyl-specific isotope labeling strategies for NMR studies of membrane proteins. In: Membrane Protein Structure and Function Characterization. Vol 1635. Springer Nature; 2017:109-123. doi:10.1007/978-1-4939-7151-0_6
View | DOI
 
[41]
2016 | Journal Article | IST-REx-ID: 8455
Kurauskas V, Crublet E, Macek P, et al. Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit. Chemical Communications. 2016;52(61):9558-9561. doi:10.1039/c6cc04484k
View | DOI
 
[40]
2016 | Journal Article | IST-REx-ID: 8453
Kurauskas V, Weber E, Hessel A, Ayala I, Marion D, Schanda P. Cross-correlated relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning R1ρ NMR measurements: Application to protein backbone dynamics measurements. The Journal of Physical Chemistry B. 2016;120(34):8905-8913. doi:10.1021/acs.jpcb.6b06129
View | DOI
 
[39]
2016 | Journal Article | IST-REx-ID: 8452
Rodrigues CDA, Henry X, Neumann E, et al. A ring-shaped conduit connects the mother cell and forespore during sporulation in Bacillus subtilis. Proceedings of the National Academy of Sciences. 2016;113(41):11585-11590. doi:10.1073/pnas.1609604113
View | DOI
 
[38]
2016 | Journal Article | IST-REx-ID: 8454
Schanda P, Ernst M. Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules. Progress in Nuclear Magnetic Resonance Spectroscopy. 2016;96(8):1-46. doi:10.1016/j.pnmrs.2016.02.001
View | DOI
 
[37]
2015 | Journal Article | IST-REx-ID: 8456
Ma P, Xue Y, Coquelle N, et al. Observing the overall rocking motion of a protein in a crystal. Nature Communications. 2015;6. doi:10.1038/ncomms9361
[Published Version] View | DOI
 
[36]
2015 | Journal Article | IST-REx-ID: 8457
Ma P, Schanda P. Conformational exchange processes in biological systems: Detection by solid-state NMR. eMagRes. 2015;4(3):699-708. doi:10.1002/9780470034590.emrstm1418
View | DOI
 
[35]
2014 | Journal Article | IST-REx-ID: 8459
Morin S, Linnet TE, Lescanne M, et al. Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. Bioinformatics. 2014;30(15):2219-2220. doi:10.1093/bioinformatics/btu166
View | Files available | DOI
 
[34]
2014 | Journal Article | IST-REx-ID: 8458
Schanda P, Triboulet S, Laguri C, et al. Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan. Journal of the American Chemical Society. 2014;136(51):17852-17860. doi:10.1021/ja5105987
View | DOI
 
[33]
2014 | Journal Article | IST-REx-ID: 8460
Ma P, Haller JD, Zajakala J, et al. Probing transient conformational states of proteins by solid-state R1ρ relaxation-dispersion NMR spectroscopy. Angewandte Chemie International Edition. 2014;53(17):4312-4317. doi:10.1002/anie.201311275
View | DOI
 
[32]
2013 | Journal Article | IST-REx-ID: 8461
Haller JD, Schanda P. Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin. Journal of Biomolecular NMR. 2013;57(3):263-280. doi:10.1007/s10858-013-9787-x
View | DOI
 
[31]
2013 | Journal Article | IST-REx-ID: 8462
Rennella E, Cutuil T, Schanda P, et al. Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure. Journal of Molecular Biology. 2013;425(15):2722-2736. doi:10.1016/j.jmb.2013.04.028
View | DOI
 
[30]
2012 | Journal Article | IST-REx-ID: 8463
Asami S, Szekely K, Schanda P, Meier BH, Reif B. Optimal degree of protonation for 1H detection of aliphatic sites in randomly deuterated proteins as a function of the MAS frequency. Journal of Biomolecular NMR. 2012;54(2):155-168. doi:10.1007/s10858-012-9659-9
View | DOI
 
[29]
2012 | Journal Article | IST-REx-ID: 8465
Tollinger M, Sivertsen AC, Meier BH, Ernst M, Schanda P. Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy. Journal of the American Chemical Society. 2012;134(36):14800-14807. doi:10.1021/ja303591y
View | DOI
 
[28]
2012 | Journal Article | IST-REx-ID: 8466
Rennella E, Cutuil T, Schanda P, Ayala I, Forge V, Brutscher B. Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate. Journal of the American Chemical Society. 2012;134(19):8066-8069. doi:10.1021/ja302598j
View | DOI
 
[27]
2012 | Journal Article | IST-REx-ID: 8467
Huber M, With O, Schanda P, Verel R, Ernst M, Meier BH. A supplementary coil for 2H decoupling with commercial HCN MAS probes. Journal of Magnetic Resonance. 2012;214:76-80. doi:10.1016/j.jmr.2011.10.010
View | DOI
 
[26]
2011 | Journal Article | IST-REx-ID: 8469
Schanda P, Meier BH, Ernst M. Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR. Journal of Magnetic Resonance. 2011;210(2):246-259. doi:10.1016/j.jmr.2011.03.015
View | DOI
 
[25]
2011 | Journal Article | IST-REx-ID: 8470
Huber M, Hiller S, Schanda P, et al. A proton-detected 4D solid-state NMR experiment for protein structure determination. ChemPhysChem. 2011;12(5):915-918. doi:10.1002/cphc.201100062
View | DOI
 
[24]
2011 | Journal Article | IST-REx-ID: 8464
Schanda P, Huber M, Boisbouvier J, Meier BH, Ernst M. Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion. Angewandte Chemie International Edition. 2011;50(46):11005-11009. doi:10.1002/anie.201103944
View | Files available | DOI
 
[23]
2011 | Journal Article | IST-REx-ID: 8468
Lalli D, Schanda P, Chowdhury A, et al. Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins. Journal of Biomolecular NMR. 2011;51(4):477-485. doi:10.1007/s10858-011-9578-1
View | DOI
 
[22]
2011 | Journal Article | IST-REx-ID: 8471
Van Melckebeke H, Schanda P, Gath J, et al. Probing water accessibility in HET-s(218–289) amyloid fibrils by solid-state NMR. Journal of Molecular Biology. 2011;405(3):765-772. doi:10.1016/j.jmb.2010.11.004
View | DOI
 
[21]
2010 | Journal Article | IST-REx-ID: 8473
Corazza A, Rennella E, Schanda P, et al. Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR. Journal of Biological Chemistry. 2010;285(8):5827-5835. doi:10.1074/jbc.m109.061168
View | DOI
 
[20]
2010 | Journal Article | IST-REx-ID: 8472
Schanda P, Meier BH, Ernst M. Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy. Journal of the American Chemical Society. 2010;132(45):15957-15967. doi:10.1021/ja100726a
View | DOI
 
[19]
2009 | Journal Article | IST-REx-ID: 8479
Gal M, Kern T, Schanda P, Frydman L, Brutscher B. An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates. Journal of Biomolecular NMR. 2009;43:1-10. doi:10.1007/s10858-008-9284-9
View | DOI
 
[18]
2009 | Journal Article | IST-REx-ID: 8478
Brüschweiler S, Schanda P, Kloiber K, et al. Direct observation of the dynamic process underlying allosteric signal transmission. Journal of the American Chemical Society. 2009;131(8):3063-3068. doi:10.1021/ja809947w
View | DOI
 
[17]
2009 | Journal Article | IST-REx-ID: 8476
Farjon J, Boisbouvier J, Schanda P, Pardi A, Simorre J-P, Brutscher B. Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution. Journal of the American Chemical Society. 2009;131(24):8571-8577. doi:10.1021/ja901633y
View | DOI
 
[16]
2009 | Journal Article | IST-REx-ID: 8477
Amero C, Schanda P, Durá MA, et al. Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies. Journal of the American Chemical Society. 2009;131(10):3448-3449. doi:10.1021/ja809880p
View | DOI
 
[15]
2009 | Journal Article | IST-REx-ID: 8474
Schanda P, Huber M, Verel R, Ernst M, Meier B. Direct detection of 3hJN’ hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy. Angewandte Chemie International Edition. 2009;48(49):9322-9325. doi:10.1002/anie.200904411
View | DOI
 
[14]
2009 | Journal Article | IST-REx-ID: 8475
Schanda P. Fast-pulsing longitudinal relaxation optimized techniques: Enriching the toolbox of fast biomolecular NMR spectroscopy. Progress in Nuclear Magnetic Resonance Spectroscopy. 2009;55(3):238-265. doi:10.1016/j.pnmrs.2009.05.002
View | DOI
 
[13]
2008 | Journal Article | IST-REx-ID: 8481
Bersch B, Favier A, Schanda P, et al. Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge. Journal of Molecular Biology. 2008;380(2):386-403. doi:10.1016/j.jmb.2008.05.017
View | DOI
 
[12]
2008 | Journal Article | IST-REx-ID: 8480
Schanda P, Brutscher B, Konrat R, Tollinger M. 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. Journal of Molecular Biology. 2008;380(4):726-741. doi:10.1016/j.jmb.2008.05.040
View | DOI
 
[11]
2008 | Journal Article | IST-REx-ID: 8482
Kern T, Schanda P, Brutscher B. Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing 2D NMR with reduced radiofrequency load. Journal of Magnetic Resonance. 2008;190(2):333-338. doi:10.1016/j.jmr.2007.11.015
View | DOI
 
[10]
2007 | Journal Article | IST-REx-ID: 8483
Schanda P, Forge V, Brutscher B. Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy. Proceedings of the National Academy of Sciences. 2007;104(27):11257-11262. doi:10.1073/pnas.0702069104
View | DOI
 
[9]
2007 | Journal Article | IST-REx-ID: 8487
Gal M, Schanda P, Brutscher B, Frydman L. UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates. Journal of the American Chemical Society. 2007;129(5):1372-1377. doi:10.1021/ja066915g
View | DOI
 
[8]
2007 | Journal Article | IST-REx-ID: 8485
Schanda P, Lescop E, Falge M, Sounier R, Boisbouvier J, Brutscher B. Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons. Journal of Biomolecular NMR. 2007;38:47-55. doi:10.1007/s10858-006-9138-2
View | DOI
 
[7]
2007 | Journal Article | IST-REx-ID: 8486
Lescop E, Schanda P, Rasia R, Brutscher B. Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy. Journal of the American Chemical Society. 2007;129(10):2756-2757. doi:10.1021/ja068949u
View | DOI
 
[6]
2007 | Journal Article | IST-REx-ID: 8484
Lescop E, Schanda P, Brutscher B. A set of BEST triple-resonance experiments for time-optimized protein resonance assignment. Journal of Magnetic Resonance. 2007;187(1):163-169. doi:10.1016/j.jmr.2007.04.002
View | DOI
 
[5]
2006 | Journal Article | IST-REx-ID: 8489
Schanda P, Forge V, Brutscher B. HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains. Magnetic Resonance in Chemistry. 2006;44(S1):S177-S184. doi:10.1002/mrc.1825
View | DOI
 
[4]
2006 | Journal Article | IST-REx-ID: 8488
Schanda P, Van Melckebeke H, Brutscher B. Speeding up three-dimensional protein NMR experiments to a few minutes. Journal of the American Chemical Society. 2006;128(28):9042-9043. doi:10.1021/ja062025p
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[3]
2006 | Journal Article | IST-REx-ID: 8490
Schanda P, Brutscher B. Hadamard frequency-encoded SOFAST-HMQC for ultrafast two-dimensional protein NMR. Journal of Magnetic Resonance. 2006;178(2):334-339. doi:10.1016/j.jmr.2005.10.007
View | DOI
 
[2]
2005 | Journal Article | IST-REx-ID: 8491
Schanda P, Kupče Ē, Brutscher B. SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds. Journal of Biomolecular NMR. 2005;33(4):199-211. doi:10.1007/s10858-005-4425-x
View | DOI
 
[1]
2005 | Journal Article | IST-REx-ID: 8492
Schanda P, Brutscher B. Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. Journal of the American Chemical Society. 2005;127(22):8014-8015. doi:10.1021/ja051306e
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