Paul Schanda

Schanda Group

81 Publications

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[81]
2023 | Journal Article | IST-REx-ID: 13095 | OA
L. Troussicot, A. Vallet, M. Molin, B. M. Burmann, and P. Schanda, “Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR,” Journal of the American Chemical Society, vol. 145, no. 19. American Chemical Society, pp. 10700–10711, 2023.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[80]
2023 | Research Data | IST-REx-ID: 12820 | OA
P. Schanda, “Research data of the publication ‘Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR.’” Institute of Science and Technology Austria, 2023.
[Published Version] View | Files available | DOI
 
[79]
2023 | Journal Article | IST-REx-ID: 12114 | OA
D. F. Gauto et al., “Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD,” Journal of Structural Biology: X, vol. 7. Elsevier, 2023.
[Published Version] View | Files available | DOI | PubMed | Europe PMC
 
[78]
2023 | Journal Article | IST-REx-ID: 13096 | OA
M. Degen et al., “Structural basis of NINJ1-mediated plasma membrane rupture in cell death,” Nature, vol. 618. Springer Nature, pp. 1065–1071, 2023.
[Published Version] View | Files available | DOI | WoS
 
[77]
2023 | Other Publication | IST-REx-ID: 14861 | OA
L. M. Becker 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, no. 19. Wiley, 2023.
[Published Version] View | Files available | DOI | Download Published Version (ext.)
 
[76]
2023 | Journal Article | IST-REx-ID: 14835 | OA
L. M. Becker et al., “Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten,” Angewandte Chemie, vol. 135, no. 19. Wiley, 2023.
[Published Version] View | Files available | DOI
 
[75]
2023 | Book Chapter | IST-REx-ID: 14847 | OA
I. Sučec and P. Schanda, “Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies,” in Biophysics of Molecular Chaperones, vol. 29, S. Hiller, M. Liu, and L. He, Eds. Royal Society of Chemistry, 2023, pp. 136–161.
[Preprint] View | DOI | Download Preprint (ext.)
 
[74]
2023 | Journal Article | IST-REx-ID: 14036 | OA
F. Napoli, L. M. Becker, and P. Schanda, “Protein dynamics detected by magic-angle spinning relaxation dispersion NMR,” Current Opinion in Structural Biology, vol. 82, no. 10. Elsevier, 2023.
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[73]
2023 | Journal Article | IST-REx-ID: 12675 | OA
L. M. Becker et al., “The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues,” Angewandte Chemie International Edition, vol. 62, no. 19. Wiley, 2023.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[72]
2023 | Research Data | IST-REx-ID: 12497 | OA
L. M. Becker and P. Schanda, “Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues.” Institute of Science and Technology Austria, 2023.
[Published Version] View | Files available | DOI
 
[71]
2022 | Journal Article | IST-REx-ID: 11179 | OA
D. F. Gauto et al., “Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR,” Nature Communications, vol. 13. Springer Nature, 2022.
[Published Version] View | Files available | DOI | WoS
 
[70]
2021 | Journal Article | IST-REx-ID: 10323 | OA
I. Sučec, B. Bersch, and P. Schanda, “How do chaperones bind (partly) unfolded client proteins?,” Frontiers in Molecular Biosciences, vol. 8. Frontiers, 2021.
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[69]
2020 | Journal Article | IST-REx-ID: 8402 | OA
H. Rampelt et al., “The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments,” BMC Biology, vol. 18. Springer Nature, 2020.
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[68]
2020 | Preprint | IST-REx-ID: 8404 | OA
K. Weinhäupl, Y. Wang, A. Hessel, M. Brennich, K. Lindorff-Larsen, and P. Schanda, “Architecture and subunit dynamics of the mitochondrial TIM9·10·12 chaperone,” bioRxiv. Cold Spring Harbor Laboratory.
[Preprint] View | DOI | Download Preprint (ext.)
 
[67]
2020 | Preprint | IST-REx-ID: 8403 | OA
I. Sučec et al., “Structural basis of client specificity in mitochondrial membrane-protein chaperones,” bioRxiv. Cold Spring Harbor Laboratory.
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[66]
2019 | Journal Article | IST-REx-ID: 8405 | OA
D. F. Gauto et al., “Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex,” Nature Communications, vol. 10. Springer Nature, 2019.
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[65]
2019 | Journal Article | IST-REx-ID: 8406 | OA
J. Felix et al., “Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors,” Science Advances, vol. 5, no. 9. American Association for the Advancement of Science, 2019.
[Published Version] View | DOI | Download Published Version (ext.)
 
[64]
2019 | Journal Article | IST-REx-ID: 8413
P. Rovó, C. A. Smith, D. Gauto, B. L. de Groot, P. Schanda, and R. Linser, “Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques,” Journal of the American Chemical Society, vol. 141, no. 2. American Chemical Society, pp. 858–869, 2019.
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[63]
2019 | Journal Article | IST-REx-ID: 8412
M. D. Shannon et al., “Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR,” ChemPhysChem, vol. 20, no. 2. Wiley, pp. 311–317, 2019.
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[62]
2019 | Journal Article | IST-REx-ID: 8411
D. Marion, D. F. Gauto, I. Ayala, K. Giandoreggio-Barranco, and P. Schanda, “Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR,” ChemPhysChem, vol. 20, no. 2. Wiley, pp. 276–284, 2019.
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[61]
2019 | Journal Article | IST-REx-ID: 8409
C. Bougault, I. Ayala, W. Vollmer, J.-P. Simorre, and P. Schanda, “Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency,” Journal of Structural Biology, vol. 206, no. 1. Elsevier, pp. 66–72, 2019.
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[60]
2019 | Journal Article | IST-REx-ID: 8407
P. Schanda, “Relaxing with liquids and solids – A perspective on biomolecular dynamics,” Journal of Magnetic Resonance, vol. 306. Elsevier, pp. 180–186, 2019.
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[59]
2019 | Journal Article | IST-REx-ID: 8410 | OA
P. Schanda and E. Y. Chekmenev, “NMR for Biological Systems,” ChemPhysChem, vol. 20, no. 2. Wiley, pp. 177–177, 2019.
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[58]
2019 | Journal Article | IST-REx-ID: 8408
D. F. Gauto 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, vol. 141, no. 28. American Chemical Society, pp. 11183–11195, 2019.
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[57]
2018 | Journal Article | IST-REx-ID: 8443
V. Kurauskas et al., “How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine,” The Journal of Physical Chemistry Letters, vol. 9, no. 5. American Chemical Society, pp. 933–938, 2018.
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[56]
2018 | Journal Article | IST-REx-ID: 8440
K. Weinhäupl 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, vol. 293, no. 22. American Society for Biochemistry & Molecular Biology, pp. 8379–8393, 2018.
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[55]
2018 | Journal Article | IST-REx-ID: 8442
C. Chipot et al., “Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies,” Chemical Reviews, vol. 118, no. 7. American Chemical Society, pp. 3559–3607, 2018.
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[54]
2018 | Journal Article | IST-REx-ID: 8441
A. Krushelnitsky, D. Gauto, D. C. Rodriguez Camargo, P. Schanda, and K. Saalwächter, “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, vol. 71, no. 1. Springer Nature, pp. 53–67, 2018.
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[53]
2018 | Journal Article | IST-REx-ID: 8439
C. Laguri et al., “Solid state NMR studies of intact lipopolysaccharide endotoxin,” ACS Chemical Biology, vol. 13, no. 8. American Chemical Society, pp. 2106–2113, 2018.
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[52]
2018 | Journal Article | IST-REx-ID: 8437
G. Mas et al., “Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle,” Science Advances, vol. 4, no. 9. American Association for the Advancement of Science, 2018.
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[51]
2018 | Journal Article | IST-REx-ID: 8436
K. Weinhäupl et al., “Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space,” Cell, vol. 175, no. 5. Elsevier, p. 1365–1379.e25, 2018.
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[50]
2018 | Journal Article | IST-REx-ID: 8438
V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, and P. Schanda, “Dynamics and interactions of AAC3 in DPC are not functionally relevant,” Nature Structural & Molecular Biology, vol. 25, no. 9. Springer Nature, pp. 745–747, 2018.
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[49]
2017 | Journal Article | IST-REx-ID: 8446
H. Fraga 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, vol. 18, no. 19. Wiley, pp. 2697–2703, 2017.
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[48]
2017 | Journal Article | IST-REx-ID: 8445
V. Kurauskas et al., “Slow conformational exchange and overall rocking motion in ubiquitin protein crystals,” Nature Communications, vol. 8. Springer Nature, 2017.
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[47]
2017 | Journal Article | IST-REx-ID: 8444
F. Dehez, P. Schanda, M. S. King, E. R. S. Kunji, and C. Chipot, “Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity,” Biophysical Journal, vol. 113, no. 11. Elsevier, pp. 2311–2315, 2017.
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[46]
2017 | Journal Article | IST-REx-ID: 8449
E. Rennella et al., “RNA binding and chaperone activity of the E.coli cold-shock protein CspA,” Nucleic Acids Research, vol. 45, no. 7. Oxford University Press, pp. 4255–4268, 2017.
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[45]
2017 | Journal Article | IST-REx-ID: 8447
D. F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, and P. Schanda, “Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals,” Solid State Nuclear Magnetic Resonance, vol. 87, no. 10. Elsevier, pp. 86–95, 2017.
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[44]
2017 | Journal Article | IST-REx-ID: 8448
R. Franco, A. Favier, P. Schanda, and B. Brutscher, “Optimized fast mixing device for real-time NMR applications,” Journal of Magnetic Resonance, vol. 281, no. 8. Elsevier, pp. 125–129, 2017.
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[43]
2017 | Journal Article | IST-REx-ID: 8451
B. Bersch, J. M. Dörr, A. Hessel, J. A. Killian, and P. Schanda, “Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native nanodiscs,” Angewandte Chemie International Edition, vol. 56, no. 9. Wiley, pp. 2508–2512, 2017.
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[42]
2017 | Book Chapter | IST-REx-ID: 8450
V. Kurauskas, P. Schanda, and R. Sounier, “Methyl-specific isotope labeling strategies for NMR studies of membrane proteins,” in Membrane protein structure and function characterization, vol. 1635, Springer Nature, 2017, pp. 109–123.
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[41]
2016 | Journal Article | IST-REx-ID: 8455
V. Kurauskas et al., “Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit,” Chemical Communications, vol. 52, no. 61. Royal Society of Chemistry, pp. 9558–9561, 2016.
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[40]
2016 | Journal Article | IST-REx-ID: 8453
V. Kurauskas, E. Weber, A. Hessel, I. Ayala, D. Marion, and P. Schanda, “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, vol. 120, no. 34. American Chemical Society, pp. 8905–8913, 2016.
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[39]
2016 | Journal Article | IST-REx-ID: 8452
C. D. A. Rodrigues et al., “A ring-shaped conduit connects the mother cell and forespore during sporulation in Bacillus subtilis,” Proceedings of the National Academy of Sciences, vol. 113, no. 41. National Academy of Sciences, pp. 11585–11590, 2016.
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[38]
2016 | Journal Article | IST-REx-ID: 8454
P. Schanda and M. Ernst, “Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules,” Progress in Nuclear Magnetic Resonance Spectroscopy, vol. 96, no. 8. Elsevier, pp. 1–46, 2016.
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[37]
2015 | Journal Article | IST-REx-ID: 8456
P. Ma et al., “Observing the overall rocking motion of a protein in a crystal,” Nature Communications, vol. 6. Springer Nature, 2015.
[Published Version] View | DOI
 
[36]
2015 | Journal Article | IST-REx-ID: 8457
P. Ma and P. Schanda, “Conformational exchange processes in biological systems: Detection by solid-state NMR,” eMagRes, vol. 4, no. 3. Wiley, pp. 699–708, 2015.
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[35]
2014 | Journal Article | IST-REx-ID: 8459
S. Morin et al., “Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data,” Bioinformatics, vol. 30, no. 15. Oxford University Press, pp. 2219–2220, 2014.
View | Files available | DOI
 
[34]
2014 | Journal Article | IST-REx-ID: 8458
P. Schanda et al., “Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan,” Journal of the American Chemical Society, vol. 136, no. 51. American Chemical Society, pp. 17852–17860, 2014.
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[33]
2014 | Journal Article | IST-REx-ID: 8460
P. Ma et al., “Probing transient conformational states of proteins by solid-state R1ρ relaxation-dispersion NMR spectroscopy,” Angewandte Chemie International Edition, vol. 53, no. 17. Wiley, pp. 4312–4317, 2014.
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[32]
2013 | Journal Article | IST-REx-ID: 8461
J. D. Haller and P. Schanda, “Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin,” Journal of Biomolecular NMR, vol. 57, no. 3. Springer Nature, pp. 263–280, 2013.
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[31]
2013 | Journal Article | IST-REx-ID: 8462
E. Rennella et al., “Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure,” Journal of Molecular Biology, vol. 425, no. 15. Elsevier, pp. 2722–2736, 2013.
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[30]
2012 | Journal Article | IST-REx-ID: 8463
S. Asami, K. Szekely, P. Schanda, B. H. Meier, and B. Reif, “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, vol. 54, no. 2. Springer Nature, pp. 155–168, 2012.
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[29]
2012 | Journal Article | IST-REx-ID: 8465
M. Tollinger, A. C. Sivertsen, B. H. Meier, M. Ernst, and P. Schanda, “Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy,” Journal of the American Chemical Society, vol. 134, no. 36. American Chemical Society, pp. 14800–14807, 2012.
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[28]
2012 | Journal Article | IST-REx-ID: 8466
E. Rennella, T. Cutuil, P. Schanda, I. Ayala, V. Forge, and B. Brutscher, “Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate,” Journal of the American Chemical Society, vol. 134, no. 19. American Chemical Society, pp. 8066–8069, 2012.
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[27]
2012 | Journal Article | IST-REx-ID: 8467
M. Huber, O. With, P. Schanda, R. Verel, M. Ernst, and B. H. Meier, “A supplementary coil for 2H decoupling with commercial HCN MAS probes,” Journal of Magnetic Resonance, vol. 214. Elsevier, pp. 76–80, 2012.
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[26]
2011 | Journal Article | IST-REx-ID: 8469
P. Schanda, B. H. Meier, and M. Ernst, “Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR,” Journal of Magnetic Resonance, vol. 210, no. 2. Elsevier, pp. 246–259, 2011.
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[25]
2011 | Journal Article | IST-REx-ID: 8470
M. Huber et al., “A proton-detected 4D solid-state NMR experiment for protein structure determination,” ChemPhysChem, vol. 12, no. 5. Wiley, pp. 915–918, 2011.
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[24]
2011 | Journal Article | IST-REx-ID: 8464
P. Schanda, M. Huber, J. Boisbouvier, B. H. Meier, and M. Ernst, “Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion,” Angewandte Chemie International Edition, vol. 50, no. 46. Wiley, pp. 11005–11009, 2011.
View | Files available | DOI
 
[23]
2011 | Journal Article | IST-REx-ID: 8468
D. Lalli et al., “Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins,” Journal of Biomolecular NMR, vol. 51, no. 4. Springer Nature, pp. 477–485, 2011.
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[22]
2011 | Journal Article | IST-REx-ID: 8471
H. Van Melckebeke et al., “Probing water accessibility in HET-s(218–289) amyloid fibrils by solid-state NMR,” Journal of Molecular Biology, vol. 405, no. 3. Elsevier, pp. 765–772, 2011.
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[21]
2010 | Journal Article | IST-REx-ID: 8473
A. Corazza 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, vol. 285, no. 8. American Society for Biochemistry & Molecular Biology, pp. 5827–5835, 2010.
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[20]
2010 | Journal Article | IST-REx-ID: 8472
P. Schanda, B. H. Meier, and M. Ernst, “Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy,” Journal of the American Chemical Society, vol. 132, no. 45. American Chemical Society, pp. 15957–15967, 2010.
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[19]
2009 | Journal Article | IST-REx-ID: 8479
M. Gal, T. Kern, P. Schanda, L. Frydman, and B. Brutscher, “An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates,” Journal of Biomolecular NMR, vol. 43. Springer Nature, pp. 1–10, 2009.
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[18]
2009 | Journal Article | IST-REx-ID: 8478
S. Brüschweiler et al., “Direct observation of the dynamic process underlying allosteric signal transmission,” Journal of the American Chemical Society, vol. 131, no. 8. American Chemical Society, pp. 3063–3068, 2009.
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[17]
2009 | Journal Article | IST-REx-ID: 8476
J. Farjon, J. Boisbouvier, P. Schanda, A. Pardi, J.-P. Simorre, and B. Brutscher, “Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution,” Journal of the American Chemical Society, vol. 131, no. 24. American Chemical Society, pp. 8571–8577, 2009.
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[16]
2009 | Journal Article | IST-REx-ID: 8477
C. Amero et al., “Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies,” Journal of the American Chemical Society, vol. 131, no. 10. American Chemical Society, pp. 3448–3449, 2009.
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[15]
2009 | Journal Article | IST-REx-ID: 8474
P. Schanda, M. Huber, R. Verel, M. Ernst, and B. Meier, “Direct detection of 3hJN’ hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy,” Angewandte Chemie International Edition, vol. 48, no. 49. Wiley, pp. 9322–9325, 2009.
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[14]
2009 | Journal Article | IST-REx-ID: 8475
P. Schanda, “Fast-pulsing longitudinal relaxation optimized techniques: Enriching the toolbox of fast biomolecular NMR spectroscopy,” Progress in Nuclear Magnetic Resonance Spectroscopy, vol. 55, no. 3. Elsevier, pp. 238–265, 2009.
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[13]
2008 | Journal Article | IST-REx-ID: 8481
B. Bersch 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, vol. 380, no. 2. Elsevier, pp. 386–403, 2008.
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[12]
2008 | Journal Article | IST-REx-ID: 8480
P. Schanda, B. Brutscher, R. Konrat, and M. Tollinger, “Folding of the KIX domain: Characterization of the equilibrium analog of a folding intermediate using 15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy,” Journal of Molecular Biology, vol. 380, no. 4. Elsevier, pp. 726–741, 2008.
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[11]
2008 | Journal Article | IST-REx-ID: 8482
T. Kern, P. Schanda, and B. Brutscher, “Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing 2D NMR with reduced radiofrequency load,” Journal of Magnetic Resonance, vol. 190, no. 2. Elsevier, pp. 333–338, 2008.
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[10]
2007 | Journal Article | IST-REx-ID: 8483
P. Schanda, V. Forge, and B. Brutscher, “Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy,” Proceedings of the National Academy of Sciences, vol. 104, no. 27. National Academy of Sciences, pp. 11257–11262, 2007.
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[9]
2007 | Journal Article | IST-REx-ID: 8487
M. Gal, P. Schanda, B. Brutscher, and L. Frydman, “UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates,” Journal of the American Chemical Society, vol. 129, no. 5. American Chemical Society, pp. 1372–1377, 2007.
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[8]
2007 | Journal Article | IST-REx-ID: 8485
P. Schanda, E. Lescop, M. Falge, R. Sounier, J. Boisbouvier, and B. Brutscher, “Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons,” Journal of Biomolecular NMR, vol. 38. Springer Nature, pp. 47–55, 2007.
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[7]
2007 | Journal Article | IST-REx-ID: 8486
E. Lescop, P. Schanda, R. Rasia, and B. Brutscher, “Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy,” Journal of the American Chemical Society, vol. 129, no. 10. American Chemical Society, pp. 2756–2757, 2007.
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[6]
2007 | Journal Article | IST-REx-ID: 8484
E. Lescop, P. Schanda, and B. Brutscher, “A set of BEST triple-resonance experiments for time-optimized protein resonance assignment,” Journal of Magnetic Resonance, vol. 187, no. 1. Elsevier, pp. 163–169, 2007.
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[5]
2006 | Journal Article | IST-REx-ID: 8489
P. Schanda, V. Forge, and B. Brutscher, “HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains,” Magnetic Resonance in Chemistry, vol. 44, no. S1. Wiley, pp. S177–S184, 2006.
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[4]
2006 | Journal Article | IST-REx-ID: 8488
P. Schanda, H. Van Melckebeke, and B. Brutscher, “Speeding up three-dimensional protein NMR experiments to a few minutes,” Journal of the American Chemical Society, vol. 128, no. 28. American Chemical Society, pp. 9042–9043, 2006.
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[3]
2006 | Journal Article | IST-REx-ID: 8490
P. Schanda and B. Brutscher, “Hadamard frequency-encoded SOFAST-HMQC for ultrafast two-dimensional protein NMR,” Journal of Magnetic Resonance, vol. 178, no. 2. Elsevier, pp. 334–339, 2006.
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[2]
2005 | Journal Article | IST-REx-ID: 8491
P. Schanda, Ē. Kupče, and B. Brutscher, “SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds,” Journal of Biomolecular NMR, vol. 33, no. 4. Springer Nature, pp. 199–211, 2005.
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[1]
2005 | Journal Article | IST-REx-ID: 8492
P. Schanda and B. Brutscher, “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, vol. 127, no. 22. American Chemical Society, pp. 8014–8015, 2005.
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81 Publications

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[81]
2023 | Journal Article | IST-REx-ID: 13095 | OA
L. Troussicot, A. Vallet, M. Molin, B. M. Burmann, and P. Schanda, “Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR,” Journal of the American Chemical Society, vol. 145, no. 19. American Chemical Society, pp. 10700–10711, 2023.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[80]
2023 | Research Data | IST-REx-ID: 12820 | OA
P. Schanda, “Research data of the publication ‘Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR.’” Institute of Science and Technology Austria, 2023.
[Published Version] View | Files available | DOI
 
[79]
2023 | Journal Article | IST-REx-ID: 12114 | OA
D. F. Gauto et al., “Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD,” Journal of Structural Biology: X, vol. 7. Elsevier, 2023.
[Published Version] View | Files available | DOI | PubMed | Europe PMC
 
[78]
2023 | Journal Article | IST-REx-ID: 13096 | OA
M. Degen et al., “Structural basis of NINJ1-mediated plasma membrane rupture in cell death,” Nature, vol. 618. Springer Nature, pp. 1065–1071, 2023.
[Published Version] View | Files available | DOI | WoS
 
[77]
2023 | Other Publication | IST-REx-ID: 14861 | OA
L. M. Becker 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, no. 19. Wiley, 2023.
[Published Version] View | Files available | DOI | Download Published Version (ext.)
 
[76]
2023 | Journal Article | IST-REx-ID: 14835 | OA
L. M. Becker et al., “Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten,” Angewandte Chemie, vol. 135, no. 19. Wiley, 2023.
[Published Version] View | Files available | DOI
 
[75]
2023 | Book Chapter | IST-REx-ID: 14847 | OA
I. Sučec and P. Schanda, “Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies,” in Biophysics of Molecular Chaperones, vol. 29, S. Hiller, M. Liu, and L. He, Eds. Royal Society of Chemistry, 2023, pp. 136–161.
[Preprint] View | DOI | Download Preprint (ext.)
 
[74]
2023 | Journal Article | IST-REx-ID: 14036 | OA
F. Napoli, L. M. Becker, and P. Schanda, “Protein dynamics detected by magic-angle spinning relaxation dispersion NMR,” Current Opinion in Structural Biology, vol. 82, no. 10. Elsevier, 2023.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[73]
2023 | Journal Article | IST-REx-ID: 12675 | OA
L. M. Becker et al., “The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues,” Angewandte Chemie International Edition, vol. 62, no. 19. Wiley, 2023.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[72]
2023 | Research Data | IST-REx-ID: 12497 | OA
L. M. Becker and P. Schanda, “Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues.” Institute of Science and Technology Austria, 2023.
[Published Version] View | Files available | DOI
 
[71]
2022 | Journal Article | IST-REx-ID: 11179 | OA
D. F. Gauto et al., “Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR,” Nature Communications, vol. 13. Springer Nature, 2022.
[Published Version] View | Files available | DOI | WoS
 
[70]
2021 | Journal Article | IST-REx-ID: 10323 | OA
I. Sučec, B. Bersch, and P. Schanda, “How do chaperones bind (partly) unfolded client proteins?,” Frontiers in Molecular Biosciences, vol. 8. Frontiers, 2021.
[Published Version] View | Files available | DOI | WoS | PubMed | Europe PMC
 
[69]
2020 | Journal Article | IST-REx-ID: 8402 | OA
H. Rampelt et al., “The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments,” BMC Biology, vol. 18. Springer Nature, 2020.
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[68]
2020 | Preprint | IST-REx-ID: 8404 | OA
K. Weinhäupl, Y. Wang, A. Hessel, M. Brennich, K. Lindorff-Larsen, and P. Schanda, “Architecture and subunit dynamics of the mitochondrial TIM9·10·12 chaperone,” bioRxiv. Cold Spring Harbor Laboratory.
[Preprint] View | DOI | Download Preprint (ext.)
 
[67]
2020 | Preprint | IST-REx-ID: 8403 | OA
I. Sučec et al., “Structural basis of client specificity in mitochondrial membrane-protein chaperones,” bioRxiv. Cold Spring Harbor Laboratory.
[Preprint] View | DOI | Download Preprint (ext.)
 
[66]
2019 | Journal Article | IST-REx-ID: 8405 | OA
D. F. Gauto et al., “Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex,” Nature Communications, vol. 10. Springer Nature, 2019.
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[65]
2019 | Journal Article | IST-REx-ID: 8406 | OA
J. Felix et al., “Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors,” Science Advances, vol. 5, no. 9. American Association for the Advancement of Science, 2019.
[Published Version] View | DOI | Download Published Version (ext.)
 
[64]
2019 | Journal Article | IST-REx-ID: 8413
P. Rovó, C. A. Smith, D. Gauto, B. L. de Groot, P. Schanda, and R. Linser, “Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques,” Journal of the American Chemical Society, vol. 141, no. 2. American Chemical Society, pp. 858–869, 2019.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[63]
2019 | Journal Article | IST-REx-ID: 8412
M. D. Shannon et al., “Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR,” ChemPhysChem, vol. 20, no. 2. Wiley, pp. 311–317, 2019.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[62]
2019 | Journal Article | IST-REx-ID: 8411
D. Marion, D. F. Gauto, I. Ayala, K. Giandoreggio-Barranco, and P. Schanda, “Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR,” ChemPhysChem, vol. 20, no. 2. Wiley, pp. 276–284, 2019.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[61]
2019 | Journal Article | IST-REx-ID: 8409
C. Bougault, I. Ayala, W. Vollmer, J.-P. Simorre, and P. Schanda, “Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency,” Journal of Structural Biology, vol. 206, no. 1. Elsevier, pp. 66–72, 2019.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[60]
2019 | Journal Article | IST-REx-ID: 8407
P. Schanda, “Relaxing with liquids and solids – A perspective on biomolecular dynamics,” Journal of Magnetic Resonance, vol. 306. Elsevier, pp. 180–186, 2019.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[59]
2019 | Journal Article | IST-REx-ID: 8410 | OA
P. Schanda and E. Y. Chekmenev, “NMR for Biological Systems,” ChemPhysChem, vol. 20, no. 2. Wiley, pp. 177–177, 2019.
[Published Version] View | DOI | Download Published Version (ext.) | PubMed | Europe PMC
 
[58]
2019 | Journal Article | IST-REx-ID: 8408
D. F. Gauto 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, vol. 141, no. 28. American Chemical Society, pp. 11183–11195, 2019.
[Submitted Version] View | DOI | PubMed | Europe PMC
 
[57]
2018 | Journal Article | IST-REx-ID: 8443
V. Kurauskas et al., “How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine,” The Journal of Physical Chemistry Letters, vol. 9, no. 5. American Chemical Society, pp. 933–938, 2018.
View | DOI
 
[56]
2018 | Journal Article | IST-REx-ID: 8440
K. Weinhäupl 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, vol. 293, no. 22. American Society for Biochemistry & Molecular Biology, pp. 8379–8393, 2018.
View | DOI
 
[55]
2018 | Journal Article | IST-REx-ID: 8442
C. Chipot et al., “Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies,” Chemical Reviews, vol. 118, no. 7. American Chemical Society, pp. 3559–3607, 2018.
View | DOI
 
[54]
2018 | Journal Article | IST-REx-ID: 8441
A. Krushelnitsky, D. Gauto, D. C. Rodriguez Camargo, P. Schanda, and K. Saalwächter, “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, vol. 71, no. 1. Springer Nature, pp. 53–67, 2018.
[Published Version] View | DOI
 
[53]
2018 | Journal Article | IST-REx-ID: 8439
C. Laguri et al., “Solid state NMR studies of intact lipopolysaccharide endotoxin,” ACS Chemical Biology, vol. 13, no. 8. American Chemical Society, pp. 2106–2113, 2018.
View | DOI
 
[52]
2018 | Journal Article | IST-REx-ID: 8437
G. Mas et al., “Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle,” Science Advances, vol. 4, no. 9. American Association for the Advancement of Science, 2018.
View | DOI
 
[51]
2018 | Journal Article | IST-REx-ID: 8436
K. Weinhäupl et al., “Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space,” Cell, vol. 175, no. 5. Elsevier, p. 1365–1379.e25, 2018.
View | DOI
 
[50]
2018 | Journal Article | IST-REx-ID: 8438
V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, and P. Schanda, “Dynamics and interactions of AAC3 in DPC are not functionally relevant,” Nature Structural & Molecular Biology, vol. 25, no. 9. Springer Nature, pp. 745–747, 2018.
View | DOI
 
[49]
2017 | Journal Article | IST-REx-ID: 8446
H. Fraga 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, vol. 18, no. 19. Wiley, pp. 2697–2703, 2017.
View | DOI
 
[48]
2017 | Journal Article | IST-REx-ID: 8445
V. Kurauskas et al., “Slow conformational exchange and overall rocking motion in ubiquitin protein crystals,” Nature Communications, vol. 8. Springer Nature, 2017.
[Published Version] View | DOI
 
[47]
2017 | Journal Article | IST-REx-ID: 8444
F. Dehez, P. Schanda, M. S. King, E. R. S. Kunji, and C. Chipot, “Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity,” Biophysical Journal, vol. 113, no. 11. Elsevier, pp. 2311–2315, 2017.
View | DOI
 
[46]
2017 | Journal Article | IST-REx-ID: 8449
E. Rennella et al., “RNA binding and chaperone activity of the E.coli cold-shock protein CspA,” Nucleic Acids Research, vol. 45, no. 7. Oxford University Press, pp. 4255–4268, 2017.
View | DOI
 
[45]
2017 | Journal Article | IST-REx-ID: 8447
D. F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, and P. Schanda, “Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals,” Solid State Nuclear Magnetic Resonance, vol. 87, no. 10. Elsevier, pp. 86–95, 2017.
View | DOI
 
[44]
2017 | Journal Article | IST-REx-ID: 8448
R. Franco, A. Favier, P. Schanda, and B. Brutscher, “Optimized fast mixing device for real-time NMR applications,” Journal of Magnetic Resonance, vol. 281, no. 8. Elsevier, pp. 125–129, 2017.
View | DOI
 
[43]
2017 | Journal Article | IST-REx-ID: 8451
B. Bersch, J. M. Dörr, A. Hessel, J. A. Killian, and P. Schanda, “Proton-detected solid-state NMR spectroscopy of a Zinc diffusion facilitator protein in native nanodiscs,” Angewandte Chemie International Edition, vol. 56, no. 9. Wiley, pp. 2508–2512, 2017.
View | DOI
 
[42]
2017 | Book Chapter | IST-REx-ID: 8450
V. Kurauskas, P. Schanda, and R. Sounier, “Methyl-specific isotope labeling strategies for NMR studies of membrane proteins,” in Membrane protein structure and function characterization, vol. 1635, Springer Nature, 2017, pp. 109–123.
View | DOI
 
[41]
2016 | Journal Article | IST-REx-ID: 8455
V. Kurauskas et al., “Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit,” Chemical Communications, vol. 52, no. 61. Royal Society of Chemistry, pp. 9558–9561, 2016.
View | DOI
 
[40]
2016 | Journal Article | IST-REx-ID: 8453
V. Kurauskas, E. Weber, A. Hessel, I. Ayala, D. Marion, and P. Schanda, “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, vol. 120, no. 34. American Chemical Society, pp. 8905–8913, 2016.
View | DOI
 
[39]
2016 | Journal Article | IST-REx-ID: 8452
C. D. A. Rodrigues et al., “A ring-shaped conduit connects the mother cell and forespore during sporulation in Bacillus subtilis,” Proceedings of the National Academy of Sciences, vol. 113, no. 41. National Academy of Sciences, pp. 11585–11590, 2016.
View | DOI
 
[38]
2016 | Journal Article | IST-REx-ID: 8454
P. Schanda and M. Ernst, “Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules,” Progress in Nuclear Magnetic Resonance Spectroscopy, vol. 96, no. 8. Elsevier, pp. 1–46, 2016.
View | DOI
 
[37]
2015 | Journal Article | IST-REx-ID: 8456
P. Ma et al., “Observing the overall rocking motion of a protein in a crystal,” Nature Communications, vol. 6. Springer Nature, 2015.
[Published Version] View | DOI
 
[36]
2015 | Journal Article | IST-REx-ID: 8457
P. Ma and P. Schanda, “Conformational exchange processes in biological systems: Detection by solid-state NMR,” eMagRes, vol. 4, no. 3. Wiley, pp. 699–708, 2015.
View | DOI
 
[35]
2014 | Journal Article | IST-REx-ID: 8459
S. Morin et al., “Relax: The analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data,” Bioinformatics, vol. 30, no. 15. Oxford University Press, pp. 2219–2220, 2014.
View | Files available | DOI
 
[34]
2014 | Journal Article | IST-REx-ID: 8458
P. Schanda et al., “Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan,” Journal of the American Chemical Society, vol. 136, no. 51. American Chemical Society, pp. 17852–17860, 2014.
View | DOI
 
[33]
2014 | Journal Article | IST-REx-ID: 8460
P. Ma et al., “Probing transient conformational states of proteins by solid-state R1ρ relaxation-dispersion NMR spectroscopy,” Angewandte Chemie International Edition, vol. 53, no. 17. Wiley, pp. 4312–4317, 2014.
View | DOI
 
[32]
2013 | Journal Article | IST-REx-ID: 8461
J. D. Haller and P. Schanda, “Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin,” Journal of Biomolecular NMR, vol. 57, no. 3. Springer Nature, pp. 263–280, 2013.
View | DOI
 
[31]
2013 | Journal Article | IST-REx-ID: 8462
E. Rennella et al., “Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure,” Journal of Molecular Biology, vol. 425, no. 15. Elsevier, pp. 2722–2736, 2013.
View | DOI
 
[30]
2012 | Journal Article | IST-REx-ID: 8463
S. Asami, K. Szekely, P. Schanda, B. H. Meier, and B. Reif, “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, vol. 54, no. 2. Springer Nature, pp. 155–168, 2012.
View | DOI
 
[29]
2012 | Journal Article | IST-REx-ID: 8465
M. Tollinger, A. C. Sivertsen, B. H. Meier, M. Ernst, and P. Schanda, “Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy,” Journal of the American Chemical Society, vol. 134, no. 36. American Chemical Society, pp. 14800–14807, 2012.
View | DOI
 
[28]
2012 | Journal Article | IST-REx-ID: 8466
E. Rennella, T. Cutuil, P. Schanda, I. Ayala, V. Forge, and B. Brutscher, “Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate,” Journal of the American Chemical Society, vol. 134, no. 19. American Chemical Society, pp. 8066–8069, 2012.
View | DOI
 
[27]
2012 | Journal Article | IST-REx-ID: 8467
M. Huber, O. With, P. Schanda, R. Verel, M. Ernst, and B. H. Meier, “A supplementary coil for 2H decoupling with commercial HCN MAS probes,” Journal of Magnetic Resonance, vol. 214. Elsevier, pp. 76–80, 2012.
View | DOI
 
[26]
2011 | Journal Article | IST-REx-ID: 8469
P. Schanda, B. H. Meier, and M. Ernst, “Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR,” Journal of Magnetic Resonance, vol. 210, no. 2. Elsevier, pp. 246–259, 2011.
View | DOI
 
[25]
2011 | Journal Article | IST-REx-ID: 8470
M. Huber et al., “A proton-detected 4D solid-state NMR experiment for protein structure determination,” ChemPhysChem, vol. 12, no. 5. Wiley, pp. 915–918, 2011.
View | DOI
 
[24]
2011 | Journal Article | IST-REx-ID: 8464
P. Schanda, M. Huber, J. Boisbouvier, B. H. Meier, and M. Ernst, “Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion,” Angewandte Chemie International Edition, vol. 50, no. 46. Wiley, pp. 11005–11009, 2011.
View | Files available | DOI
 
[23]
2011 | Journal Article | IST-REx-ID: 8468
D. Lalli et al., “Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins,” Journal of Biomolecular NMR, vol. 51, no. 4. Springer Nature, pp. 477–485, 2011.
View | DOI
 
[22]
2011 | Journal Article | IST-REx-ID: 8471
H. Van Melckebeke et al., “Probing water accessibility in HET-s(218–289) amyloid fibrils by solid-state NMR,” Journal of Molecular Biology, vol. 405, no. 3. Elsevier, pp. 765–772, 2011.
View | DOI
 
[21]
2010 | Journal Article | IST-REx-ID: 8473
A. Corazza 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, vol. 285, no. 8. American Society for Biochemistry & Molecular Biology, pp. 5827–5835, 2010.
View | DOI
 
[20]
2010 | Journal Article | IST-REx-ID: 8472
P. Schanda, B. H. Meier, and M. Ernst, “Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy,” Journal of the American Chemical Society, vol. 132, no. 45. American Chemical Society, pp. 15957–15967, 2010.
View | DOI
 
[19]
2009 | Journal Article | IST-REx-ID: 8479
M. Gal, T. Kern, P. Schanda, L. Frydman, and B. Brutscher, “An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates,” Journal of Biomolecular NMR, vol. 43. Springer Nature, pp. 1–10, 2009.
View | DOI
 
[18]
2009 | Journal Article | IST-REx-ID: 8478
S. Brüschweiler et al., “Direct observation of the dynamic process underlying allosteric signal transmission,” Journal of the American Chemical Society, vol. 131, no. 8. American Chemical Society, pp. 3063–3068, 2009.
View | DOI
 
[17]
2009 | Journal Article | IST-REx-ID: 8476
J. Farjon, J. Boisbouvier, P. Schanda, A. Pardi, J.-P. Simorre, and B. Brutscher, “Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution,” Journal of the American Chemical Society, vol. 131, no. 24. American Chemical Society, pp. 8571–8577, 2009.
View | DOI
 
[16]
2009 | Journal Article | IST-REx-ID: 8477
C. Amero et al., “Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies,” Journal of the American Chemical Society, vol. 131, no. 10. American Chemical Society, pp. 3448–3449, 2009.
View | DOI
 
[15]
2009 | Journal Article | IST-REx-ID: 8474
P. Schanda, M. Huber, R. Verel, M. Ernst, and B. Meier, “Direct detection of 3hJN’ hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy,” Angewandte Chemie International Edition, vol. 48, no. 49. Wiley, pp. 9322–9325, 2009.
View | DOI
 
[14]
2009 | Journal Article | IST-REx-ID: 8475
P. Schanda, “Fast-pulsing longitudinal relaxation optimized techniques: Enriching the toolbox of fast biomolecular NMR spectroscopy,” Progress in Nuclear Magnetic Resonance Spectroscopy, vol. 55, no. 3. Elsevier, pp. 238–265, 2009.
View | DOI
 
[13]
2008 | Journal Article | IST-REx-ID: 8481
B. Bersch 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, vol. 380, no. 2. Elsevier, pp. 386–403, 2008.
View | DOI
 
[12]
2008 | Journal Article | IST-REx-ID: 8480
P. Schanda, B. Brutscher, R. Konrat, and M. Tollinger, “Folding of the KIX domain: Characterization of the equilibrium analog of a folding intermediate using 15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy,” Journal of Molecular Biology, vol. 380, no. 4. Elsevier, pp. 726–741, 2008.
View | DOI
 
[11]
2008 | Journal Article | IST-REx-ID: 8482
T. Kern, P. Schanda, and B. Brutscher, “Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing 2D NMR with reduced radiofrequency load,” Journal of Magnetic Resonance, vol. 190, no. 2. Elsevier, pp. 333–338, 2008.
View | DOI
 
[10]
2007 | Journal Article | IST-REx-ID: 8483
P. Schanda, V. Forge, and B. Brutscher, “Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy,” Proceedings of the National Academy of Sciences, vol. 104, no. 27. National Academy of Sciences, pp. 11257–11262, 2007.
View | DOI
 
[9]
2007 | Journal Article | IST-REx-ID: 8487
M. Gal, P. Schanda, B. Brutscher, and L. Frydman, “UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates,” Journal of the American Chemical Society, vol. 129, no. 5. American Chemical Society, pp. 1372–1377, 2007.
View | DOI
 
[8]
2007 | Journal Article | IST-REx-ID: 8485
P. Schanda, E. Lescop, M. Falge, R. Sounier, J. Boisbouvier, and B. Brutscher, “Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons,” Journal of Biomolecular NMR, vol. 38. Springer Nature, pp. 47–55, 2007.
View | DOI
 
[7]
2007 | Journal Article | IST-REx-ID: 8486
E. Lescop, P. Schanda, R. Rasia, and B. Brutscher, “Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy,” Journal of the American Chemical Society, vol. 129, no. 10. American Chemical Society, pp. 2756–2757, 2007.
View | DOI
 
[6]
2007 | Journal Article | IST-REx-ID: 8484
E. Lescop, P. Schanda, and B. Brutscher, “A set of BEST triple-resonance experiments for time-optimized protein resonance assignment,” Journal of Magnetic Resonance, vol. 187, no. 1. Elsevier, pp. 163–169, 2007.
View | DOI
 
[5]
2006 | Journal Article | IST-REx-ID: 8489
P. Schanda, V. Forge, and B. Brutscher, “HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains,” Magnetic Resonance in Chemistry, vol. 44, no. S1. Wiley, pp. S177–S184, 2006.
View | DOI
 
[4]
2006 | Journal Article | IST-REx-ID: 8488
P. Schanda, H. Van Melckebeke, and B. Brutscher, “Speeding up three-dimensional protein NMR experiments to a few minutes,” Journal of the American Chemical Society, vol. 128, no. 28. American Chemical Society, pp. 9042–9043, 2006.
View | DOI
 
[3]
2006 | Journal Article | IST-REx-ID: 8490
P. Schanda and B. Brutscher, “Hadamard frequency-encoded SOFAST-HMQC for ultrafast two-dimensional protein NMR,” Journal of Magnetic Resonance, vol. 178, no. 2. Elsevier, pp. 334–339, 2006.
View | DOI
 
[2]
2005 | Journal Article | IST-REx-ID: 8491
P. Schanda, Ē. Kupče, and B. Brutscher, “SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds,” Journal of Biomolecular NMR, vol. 33, no. 4. Springer Nature, pp. 199–211, 2005.
View | DOI
 
[1]
2005 | Journal Article | IST-REx-ID: 8492
P. Schanda and B. Brutscher, “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, vol. 127, no. 22. American Chemical Society, pp. 8014–8015, 2005.
View | DOI
 
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