[{"language":[{"iso":"eng"}],"doi":"10.1007/s10858-018-0191-4","date_published":"2018-05-30T00:00:00Z","quality_controlled":"1","article_type":"original","page":"53-67","publication":"Journal of Biomolecular NMR","citation":{"apa":"Krushelnitsky, A., Gauto, D., Rodriguez Camargo, D. C., Schanda, P., & Saalwächter, K. (2018). 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. Springer Nature. https://doi.org/10.1007/s10858-018-0191-4","ieee":"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.","ista":"Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K. 2018. 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. 71(1), 53–67.","ama":"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","chicago":"Krushelnitsky, Alexey, Diego Gauto, Diana C. Rodriguez Camargo, Paul Schanda, and Kay 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. Springer Nature, 2018. https://doi.org/10.1007/s10858-018-0191-4.","short":"A. Krushelnitsky, D. Gauto, D.C. Rodriguez Camargo, P. Schanda, K. Saalwächter, Journal of Biomolecular NMR 71 (2018) 53–67.","mla":"Krushelnitsky, Alexey, et al. “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, 2018, pp. 53–67, doi:10.1007/s10858-018-0191-4."},"month":"05","day":"30","article_processing_charge":"No","publication_identifier":{"issn":["0925-2738","1573-5001"]},"date_updated":"2021-01-12T08:19:17Z","date_created":"2020-09-18T10:05:28Z","volume":71,"oa_version":"Published Version","author":[{"full_name":"Krushelnitsky, Alexey","last_name":"Krushelnitsky","first_name":"Alexey"},{"first_name":"Diego","last_name":"Gauto","full_name":"Gauto, Diego"},{"full_name":"Rodriguez Camargo, Diana C.","first_name":"Diana C.","last_name":"Rodriguez Camargo"},{"full_name":"Schanda, Paul","last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"first_name":"Kay","last_name":"Saalwächter","full_name":"Saalwächter, Kay"}],"status":"public","title":"Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals","publication_status":"published","intvolume":" 71","publisher":"Springer Nature","_id":"8441","year":"2018","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","abstract":[{"lang":"eng","text":"Solid-state near-rotary-resonance measurements of the spin–lattice relaxation rate in the rotating frame (R1ρ) is a powerful NMR technique for studying molecular dynamics in the microsecond time scale. The small difference between the spin-lock (SL) and magic-angle-spinning (MAS) frequencies allows sampling very slow motions, at the same time it brings up some methodological challenges. In this work, several issues affecting correct measurements and analysis of 15N R1ρ data are considered in detail. Among them are signal amplitude as a function of the difference between SL and MAS frequencies, “dead time” in the initial part of the relaxation decay caused by transient spin-dynamic oscillations, measurements under HORROR condition and proper treatment of the multi-exponential relaxation decays. The multiple 15N R1ρ measurements at different SL fields and temperatures have been conducted in 1D mode (i.e. without site-specific resolution) for a set of four different microcrystalline protein samples (GB1, SH3, MPD-ubiquitin and cubic-PEG-ubiquitin) to study the overall protein rocking in a crystal. While the amplitude of this motion varies very significantly, its correlation time for all four sample is practically the same, 30–50 μs. The amplitude of the rocking motion correlates with the packing density of a protein crystal. It has been suggested that the rocking motion is not diffusive but likely a jump-like dynamic process."}],"issue":"1","type":"journal_article"},{"language":[{"iso":"eng"}],"date_published":"2013-10-09T00:00:00Z","doi":"10.1007/s10858-013-9787-x","page":"263-280","article_type":"original","quality_controlled":"1","citation":{"mla":"Haller, Jens D., and Paul Schanda. “Amplitudes and Time Scales of Picosecond-to-Microsecond Motion in Proteins Studied by Solid-State NMR: A Critical Evaluation of Experimental Approaches and Application to Crystalline Ubiquitin.” Journal of Biomolecular NMR, vol. 57, no. 3, Springer Nature, 2013, pp. 263–80, doi:10.1007/s10858-013-9787-x.","short":"J.D. Haller, P. Schanda, Journal of Biomolecular NMR 57 (2013) 263–280.","chicago":"Haller, Jens D., and Paul Schanda. “Amplitudes and Time Scales of Picosecond-to-Microsecond Motion in Proteins Studied by Solid-State NMR: A Critical Evaluation of Experimental Approaches and Application to Crystalline Ubiquitin.” Journal of Biomolecular NMR. Springer Nature, 2013. https://doi.org/10.1007/s10858-013-9787-x.","ama":"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","ista":"Haller JD, Schanda P. 2013. 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. 57(3), 263–280.","ieee":"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.","apa":"Haller, J. D., & Schanda, P. (2013). 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. Springer Nature. https://doi.org/10.1007/s10858-013-9787-x"},"publication":"Journal of Biomolecular NMR","publication_identifier":{"issn":["0925-2738","1573-5001"]},"article_processing_charge":"No","month":"10","day":"09","keyword":["Spectroscopy","Biochemistry"],"oa_version":"None","volume":57,"date_created":"2020-09-18T10:09:05Z","date_updated":"2021-01-12T08:19:26Z","author":[{"last_name":"Haller","first_name":"Jens D.","full_name":"Haller, Jens D."},{"full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","last_name":"Schanda"}],"intvolume":" 57","publisher":"Springer Nature","publication_status":"published","title":"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","status":"public","_id":"8461","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2013","extern":"1","issue":"3","abstract":[{"lang":"eng","text":"Solid-state NMR provides insight into protein motion over time scales ranging from picoseconds to seconds. While in solution state the methodology to measure protein dynamics is well established, there is currently no such consensus protocol for measuring dynamics in solids. In this article, we perform a detailed investigation of measurement protocols for fast motions, i.e. motions ranging from picoseconds to a few microseconds, which is the range covered by dipolar coupling and relaxation experiments. We perform a detailed theoretical investigation how dipolar couplings and relaxation data can provide information about amplitudes and time scales of local motion. We show that the measurement of dipolar couplings is crucial for obtaining accurate motional parameters, while systematic errors are found when only relaxation data are used. Based on this realization, we investigate how the REDOR experiment can provide such data in a very accurate manner. We identify that with accurate rf calibration, and explicit consideration of rf field inhomogeneities, one can obtain highly accurate absolute order parameters. We then perform joint model-free analyses of 6 relaxation data sets and dipolar couplings, based on previously existing, as well as new data sets on microcrystalline ubiquitin. We show that nanosecond motion can be detected primarily in loop regions, and compare solid-state data to solution-state relaxation and RDC analyses. The protocols investigated here will serve as a useful basis towards the establishment of a routine protocol for the characterization of ps–μs motions in proteins by solid-state NMR."}],"type":"journal_article"},{"author":[{"full_name":"Asami, Sam","last_name":"Asami","first_name":"Sam"},{"full_name":"Szekely, Kathrin","first_name":"Kathrin","last_name":"Szekely"},{"first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"},{"full_name":"Meier, Beat H.","first_name":"Beat H.","last_name":"Meier"},{"last_name":"Reif","first_name":"Bernd","full_name":"Reif, Bernd"}],"date_created":"2020-09-18T10:09:18Z","date_updated":"2021-01-12T08:19:27Z","oa_version":"None","volume":54,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"8463","year":"2012","status":"public","publication_status":"published","title":"Optimal degree of protonation for 1H detection of aliphatic sites in randomly deuterated proteins as a function of the MAS frequency","publisher":"Springer Nature","intvolume":" 54","abstract":[{"lang":"eng","text":"The 1H dipolar network, which is the major obstacle for applying proton detection in the solid-state, can be reduced by deuteration, employing the RAP (Reduced Adjoining Protonation) labeling scheme, which yields random protonation at non-exchangeable sites. We present here a systematic study on the optimal degree of random sidechain protonation in RAP samples as a function of the MAS (magic angle spinning) frequency. In particular, we compare 1H sensitivity and linewidth of a microcrystalline protein, the SH3 domain of chicken α-spectrin, for samples, prepared with 5–25 % H2O in the E. coli growth medium, in the MAS frequency range of 20–60 kHz. At an external field of 19.96 T (850 MHz), we find that using a proton concentration between 15 and 25 % in the M9 medium yields the best compromise in terms of sensitivity and resolution, with an achievable average 1H linewidth on the order of 40–50 Hz. Comparing sensitivities at a MAS frequency of 60 versus 20 kHz, a gain in sensitivity by a factor of 4–4.5 is observed in INEPT-based 1H detected 1D 1H,13C correlation experiments. In total, we find that spectra recorded with a 1.3 mm rotor at 60 kHz have almost the same sensitivity as spectra recorded with a fully packed 3.2 mm rotor at 20 kHz, even though ~20× less material is employed. The improved sensitivity is attributed to 1H line narrowing due to fast MAS and to the increased efficiency of the 1.3 mm coil."}],"issue":"2","extern":"1","type":"journal_article","doi":"10.1007/s10858-012-9659-9","date_published":"2012-08-23T00:00:00Z","language":[{"iso":"eng"}],"publication":"Journal of Biomolecular NMR","citation":{"ama":"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","ista":"Asami S, Szekely K, Schanda P, Meier BH, Reif B. 2012. 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. 54(2), 155–168.","apa":"Asami, S., Szekely, K., Schanda, P., Meier, B. H., & Reif, B. (2012). 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. Springer Nature. https://doi.org/10.1007/s10858-012-9659-9","ieee":"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.","mla":"Asami, Sam, et al. “Optimal Degree of Protonation for 1H Detection of Aliphatic Sites in Randomly Deuterated Proteins as a Function of the MAS Frequency.” Journal of Biomolecular NMR, vol. 54, no. 2, Springer Nature, 2012, pp. 155–68, doi:10.1007/s10858-012-9659-9.","short":"S. Asami, K. Szekely, P. Schanda, B.H. Meier, B. Reif, Journal of Biomolecular NMR 54 (2012) 155–168.","chicago":"Asami, Sam, Kathrin Szekely, Paul Schanda, Beat H. Meier, and Bernd 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. Springer Nature, 2012. https://doi.org/10.1007/s10858-012-9659-9."},"article_type":"original","quality_controlled":"1","page":"155-168","month":"08","day":"23","publication_identifier":{"issn":["0925-2738","1573-5001"]},"article_processing_charge":"No"},{"type":"journal_article","issue":"4","extern":"1","year":"2011","_id":"8468","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","intvolume":" 51","publisher":"Springer Nature","publication_status":"published","status":"public","title":"Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins","author":[{"full_name":"Lalli, Daniela","first_name":"Daniela","last_name":"Lalli"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","last_name":"Schanda","full_name":"Schanda, Paul"},{"first_name":"Anup","last_name":"Chowdhury","full_name":"Chowdhury, Anup"},{"full_name":"Retel, Joren","last_name":"Retel","first_name":"Joren"},{"first_name":"Matthias","last_name":"Hiller","full_name":"Hiller, Matthias"},{"first_name":"Victoria A.","last_name":"Higman","full_name":"Higman, Victoria A."},{"full_name":"Handel, Lieselotte","last_name":"Handel","first_name":"Lieselotte"},{"last_name":"Agarwal","first_name":"Vipin","full_name":"Agarwal, Vipin"},{"full_name":"Reif, Bernd","first_name":"Bernd","last_name":"Reif"},{"full_name":"van Rossum, Barth","first_name":"Barth","last_name":"van Rossum"},{"full_name":"Akbey, Ümit","last_name":"Akbey","first_name":"Ümit"},{"last_name":"Oschkinat","first_name":"Hartmut","full_name":"Oschkinat, Hartmut"}],"volume":51,"oa_version":"None","date_updated":"2021-01-12T08:19:29Z","date_created":"2020-09-18T10:10:43Z","publication_identifier":{"issn":["0925-2738","1573-5001"]},"article_processing_charge":"No","month":"10","day":"25","citation":{"short":"D. Lalli, P. Schanda, A. Chowdhury, J. Retel, M. Hiller, V.A. Higman, L. Handel, V. Agarwal, B. Reif, B. van Rossum, Ü. Akbey, H. Oschkinat, Journal of Biomolecular NMR 51 (2011) 477–485.","mla":"Lalli, Daniela, 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, 2011, pp. 477–85, doi:10.1007/s10858-011-9578-1.","chicago":"Lalli, Daniela, Paul Schanda, Anup Chowdhury, Joren Retel, Matthias Hiller, Victoria A. Higman, Lieselotte Handel, et al. “Three-Dimensional Deuterium-Carbon Correlation Experiments for High-Resolution Solid-State MAS NMR Spectroscopy of Large Proteins.” Journal of Biomolecular NMR. Springer Nature, 2011. https://doi.org/10.1007/s10858-011-9578-1.","ama":"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","apa":"Lalli, D., Schanda, P., Chowdhury, A., Retel, J., Hiller, M., Higman, V. A., … Oschkinat, H. (2011). Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-011-9578-1","ieee":"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.","ista":"Lalli D, Schanda P, Chowdhury A, Retel J, Hiller M, Higman VA, Handel L, Agarwal V, Reif B, van Rossum B, Akbey Ü, Oschkinat H. 2011. Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins. Journal of Biomolecular NMR. 51(4), 477–485."},"publication":"Journal of Biomolecular NMR","page":"477-485","article_type":"original","quality_controlled":"1","doi":"10.1007/s10858-011-9578-1","date_published":"2011-10-25T00:00:00Z","language":[{"iso":"eng"}]},{"keyword":["Spectroscopy","Biochemistry"],"publication_identifier":{"issn":["0925-2738","1573-5001"]},"article_processing_charge":"No","month":"01","day":"01","citation":{"ama":"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","ieee":"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.","apa":"Gal, M., Kern, T., Schanda, P., Frydman, L., & Brutscher, B. (2009). An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-008-9284-9","ista":"Gal M, Kern T, Schanda P, Frydman L, Brutscher B. 2009. An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates. Journal of Biomolecular NMR. 43, 1–10.","short":"M. Gal, T. Kern, P. Schanda, L. Frydman, B. Brutscher, Journal of Biomolecular NMR 43 (2009) 1–10.","mla":"Gal, Maayan, et al. “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, 2009, pp. 1–10, doi:10.1007/s10858-008-9284-9.","chicago":"Gal, Maayan, Thomas Kern, Paul Schanda, Lucio Frydman, and Bernhard Brutscher. “An Improved Ultrafast 2D NMR Experiment: Towards Atom-Resolved Real-Time Studies of Protein Kinetics at Multi-Hz Rates.” Journal of Biomolecular NMR. Springer Nature, 2009. https://doi.org/10.1007/s10858-008-9284-9."},"publication":"Journal of Biomolecular NMR","page":"1-10","article_type":"original","quality_controlled":"1","date_published":"2009-01-01T00:00:00Z","doi":"10.1007/s10858-008-9284-9","language":[{"iso":"eng"}],"type":"journal_article","abstract":[{"lang":"eng","text":"Multidimensional NMR spectroscopy is a well-established technique for the characterization of structure and fast-time-scale dynamics of highly populated ground states of biological macromolecules. The investigation of short-lived excited states that are important for molecular folding, misfolding and function, however, remains a challenge for modern biomolecular NMR techniques. Off-equilibrium real-time kinetic NMR methods allow direct observation of conformational or chemical changes by following peak positions and intensities in a series of spectra recorded during a kinetic event. Because standard multidimensional NMR methods required to yield sufficient atom-resolution are intrinsically time-consuming, many interesting phenomena are excluded from real-time NMR analysis. Recently, spatially encoded ultrafast 2D NMR techniques have been proposed that allow one to acquire a 2D NMR experiment within a single transient. In addition, when combined with the SOFAST technique, such ultrafast experiments can be repeated at high rates. One of the problems detected for such ultrafast protein NMR experiments is related to the heteronuclear decoupling during detection with interferences between the pulses and the oscillatory magnetic field gradients arising in this scheme. Here we present a method for improved ultrafast data acquisition yielding higher signal to noise and sharper lines in single-scan 2D NMR spectra. In combination with a fast-mixing device, the recording of 1H–15N correlation spectra with repetition rates of up to a few Hertz becomes feasible, enabling real-time studies of protein kinetics occurring on time scales down to a few seconds."}],"extern":"1","year":"2009","_id":"8479","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Springer Nature","intvolume":" 43","status":"public","publication_status":"published","title":"An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates","author":[{"full_name":"Gal, Maayan","last_name":"Gal","first_name":"Maayan"},{"last_name":"Kern","first_name":"Thomas","full_name":"Kern, Thomas"},{"first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"},{"full_name":"Frydman, Lucio","first_name":"Lucio","last_name":"Frydman"},{"full_name":"Brutscher, Bernhard","first_name":"Bernhard","last_name":"Brutscher"}],"oa_version":"None","volume":43,"date_created":"2020-09-18T10:12:20Z","date_updated":"2021-01-12T08:19:33Z"},{"language":[{"iso":"eng"}],"doi":"10.1007/s10858-006-9138-2","date_published":"2007-03-08T00:00:00Z","article_type":"original","quality_controlled":"1","page":"47-55","publication":"Journal of Biomolecular NMR","citation":{"ieee":"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.","apa":"Schanda, P., Lescop, E., Falge, M., Sounier, R., Boisbouvier, J., & Brutscher, B. (2007). Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-006-9138-2","ista":"Schanda P, Lescop E, Falge M, Sounier R, Boisbouvier J, Brutscher B. 2007. Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons. Journal of Biomolecular NMR. 38, 47–55.","ama":"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","chicago":"Schanda, Paul, Ewen Lescop, Mirjam Falge, Rémy Sounier, Jérôme Boisbouvier, and Bernhard Brutscher. “Sensitivity-Optimized Experiment for the Measurement of Residual Dipolar Couplings between Amide Protons.” Journal of Biomolecular NMR. Springer Nature, 2007. https://doi.org/10.1007/s10858-006-9138-2.","short":"P. Schanda, E. Lescop, M. Falge, R. Sounier, J. Boisbouvier, B. Brutscher, Journal of Biomolecular NMR 38 (2007) 47–55.","mla":"Schanda, Paul, et al. “Sensitivity-Optimized Experiment for the Measurement of Residual Dipolar Couplings between Amide Protons.” Journal of Biomolecular NMR, vol. 38, Springer Nature, 2007, pp. 47–55, doi:10.1007/s10858-006-9138-2."},"month":"03","day":"08","publication_identifier":{"issn":["0925-2738","1573-5001"]},"article_processing_charge":"No","keyword":["Spectroscopy","Biochemistry"],"date_created":"2020-09-18T10:13:12Z","date_updated":"2021-01-12T08:19:36Z","volume":38,"oa_version":"None","author":[{"full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul"},{"first_name":"Ewen","last_name":"Lescop","full_name":"Lescop, Ewen"},{"full_name":"Falge, Mirjam","last_name":"Falge","first_name":"Mirjam"},{"full_name":"Sounier, Rémy","first_name":"Rémy","last_name":"Sounier"},{"first_name":"Jérôme","last_name":"Boisbouvier","full_name":"Boisbouvier, Jérôme"},{"last_name":"Brutscher","first_name":"Bernhard","full_name":"Brutscher, Bernhard"}],"title":"Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons","publication_status":"published","status":"public","intvolume":" 38","publisher":"Springer Nature","_id":"8485","year":"2007","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","abstract":[{"lang":"eng","text":"High signal to noise is a necessity for the quantification of NMR spectral parameters to be translated into accurate and precise restraints on protein structure and dynamics. An important source of long-range structural information is obtained from 1H–1H residual dipolar couplings (RDCs) measured for weakly aligned molecules. For sensitivity reasons, such measurements are generally performed on highly deuterated protein samples. Here we show that high sensitivity is also obtained for protonated protein samples if the pulse schemes are optimized in terms of longitudinal relaxation efficiency and J-mismatch compensated coherence transfer. The new sensitivity-optimized quantitative J-correlation experiment yields important signal gains reaching factors of 1.5 to 8 for individual correlation peaks when compared to previously proposed pulse schemes."}],"type":"journal_article"},{"author":[{"full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul"},{"last_name":"Kupče","first_name":"Ēriks","full_name":"Kupče, Ēriks"},{"last_name":"Brutscher","first_name":"Bernhard","full_name":"Brutscher, Bernhard"}],"date_updated":"2021-01-12T08:19:38Z","date_created":"2020-09-18T10:13:59Z","volume":33,"oa_version":"None","_id":"8491","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2005","publication_status":"published","title":"SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds","status":"public","publisher":"Springer Nature","intvolume":" 33","abstract":[{"text":"Fast multidimensional NMR with a time resolution of a few seconds provides a new tool for high throughput screening and site-resolved real-time studies of kinetic molecular processes by NMR. Recently we have demonstrated the feasibility to record protein 1H–15N correlation spectra in a few seconds of acquisition time using a new SOFAST-HMQC experiment (Schanda and Brutscher (2005) J. Am. Chem. Soc. 127, 8014). Here, we investigate in detail the performance of SOFAST-HMQC to record 1H–15N and 1H−13C correlation spectra of proteins of different size and at different magnetic field strengths. Compared to standard 1H–15N correlation experiments SOFAST-HMQC provides a significant gain in sensitivity, especially for fast repetition rates. Guidelines are provided on how to set up SOFAST-HMQC experiments for a given protein sample. In addition, an alternative pulse scheme, IPAP-SOFAST-HMQC is presented that allows application on NMR spectrometers equipped with cryogenic probes, and fast measurement of one-bond 1H–13C and 1H–15N scalar and residual dipolar coupling constants.","lang":"eng"}],"issue":"4","extern":"1","type":"journal_article","date_published":"2005-12-01T00:00:00Z","doi":"10.1007/s10858-005-4425-x","language":[{"iso":"eng"}],"publication":"Journal of Biomolecular NMR","citation":{"mla":"Schanda, Paul, et al. “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, 2005, pp. 199–211, doi:10.1007/s10858-005-4425-x.","short":"P. Schanda, Ē. Kupče, B. Brutscher, Journal of Biomolecular NMR 33 (2005) 199–211.","chicago":"Schanda, Paul, Ēriks Kupče, and Bernhard Brutscher. “SOFAST-HMQC Experiments for Recording Two-Dimensional Deteronuclear Correlation Spectra of Proteins within a Few Seconds.” Journal of Biomolecular NMR. Springer Nature, 2005. https://doi.org/10.1007/s10858-005-4425-x.","ama":"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","ista":"Schanda P, Kupče Ē, Brutscher B. 2005. SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds. Journal of Biomolecular NMR. 33(4), 199–211.","ieee":"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.","apa":"Schanda, P., Kupče, Ē., & Brutscher, B. (2005). SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-005-4425-x"},"quality_controlled":"1","article_type":"original","page":"199-211","month":"12","day":"01","article_processing_charge":"No","publication_identifier":{"issn":["0925-2738","1573-5001"]},"keyword":["Spectroscopy","Biochemistry"]}]