D. F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, and P. Schanda, “Protein conformational dynamics studied by 15N and 1H<1 relaxation dispersion: Application to wild-type and A ubiquitin crystals,” Solid State Nuclear Magnetic Resonance, vol. 87, no. 10. Elsevier, pp. 86–95, 2017.
LibreCat: https://research-explorer.ista.ac.at/record/8447
DOI: 10.1016/j.ssnmr.2017.04.002

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.
LibreCat: https://research-explorer.ista.ac.at/record/8448
DOI: 10.1016/j.jmr.2017.05.016

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.
LibreCat: https://research-explorer.ista.ac.at/record/8469
DOI: 10.1016/j.jmr.2011.03.015

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.
LibreCat: https://research-explorer.ista.ac.at/record/8482
DOI: 10.1016/j.jmr.2007.11.015

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.
LibreCat: https://research-explorer.ista.ac.at/record/8490
DOI: 10.1016/j.jmr.2005.10.007