Carlström, G., Elvander, F., Swärd, J., Jakobsson, A., and Akke, M.:
Rapid NMR relaxation measurements using optimal nonuniform sampling of
multidimensional accordion data analyzed by a sparse reconstruction method,
J. Phys. Chem. A, 123, 5718–5723, https://doi.org/10.1021/acs.jpca.9b04152, 2019.
Carr, P. A., Fearing, D. A., and Palmer, A. G.: 3D Accordion Spectroscopy for
Measuring 15N and 13CO Relaxation Rates in Poorly Resolved NMR Spectra, J.
Magn. Reson., 132, 25–33, https://doi.org/10.1006/jmre.1998.1374, 1998.
Chen, K. and Tjandra, N.: Direct measurements of protein backbone 15N spin
relaxation rates from peak line-width using a fully-relaxed Accordion 3D
HNCO experiment, J. Magn. Reson., 197, 71–76,
https://doi.org/10.1016/j.jmr.2008.12.001, 2009.
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax,
A.: NMRPipe: A multidimensional spectral processing system based on UNIX
pipes, J. Biomol. NMR, 6, 277–293, 1995.
Diehl, C., Genheden, S., Modig, K., Ryde, U., and Akke, M.: Conformational
entropy changes upon lactose binding to the carbohydrate recognition domain
of galectin-3, J. Biomol. NMR, 45, 157–169, https://doi.org/10.1007/s10858-009-9356-5,
2009.
Diehl, C., Engström, O., Delaine, T., Håkansson, M., Genheden, S.,
Modig, K., Leffler, H., Ryde, U., Nilsson, U. J., and Akke, M.: Protein
flexibility and conformational entropy in ligand design targeting the
carbohydrate recognition domain of galectin-3, J. Am. Chem. Soc., 132,
14577–14589, 2010.
East, K. W., Delaglio, F., and Lisi, G. P.: A simple approach for
reconstruction of non-uniformly sampled pseudo-3D NMR data for accurate
measurement of spin relaxation parameters, J. Biomol. NMR,
https://doi.org/10.1007/s10858-021-00369-7, online first, 2021.
Farrow, N. A., Zhang, O., Forman-Kay, J. D., and Kay, L. E.: Comparison of
the backbone dynamics of a folded and an unfolded SH3 domain existing in
equilibrium in aqueous buffer, Biochemistry, 34, 868–878, 1995.
Gołowicz, D., Kasprzak, P., Orekhov, V., and Kazimierczuk, K.: Fast
time-resolved NMR with non-uniform sampling, Prog. Nucl. Magn. Reson.
Spectrosc., 116, 40–55, https://doi.org/10.1016/j.pnmrs.2019.09.003, 2020.
Grzesiek, S. and Bax, A.: The importance of not saturating H
2O in protein
NMR. Application to sensitivity enhancement and NOE measurements, J. Am.
Chem. Soc., 115, 12593–12594, 1993.
Hansen, D. F. and Kay, L. E.: Improved magnetization alignment schemes for
spin-lock relaxation experiments, J. Biomol. NMR, 37, 245–255,
https://doi.org/10.1007/s10858-006-9126-6, 2007.
Harden, B. J. and Frueh, D. P.: SARA: A software environment for the
analysis of relaxation data acquired with accordion spectroscopy, J. Biomol.
NMR, 58, 83–99, https://doi.org/10.1007/s10858-013-9807-x, 2014.
Hyberts, S. G., Takeuchi, K., and Wagner, G.: Poisson-gap sampling and
forward maximum entropy reconstruction for enhancing the resolution and
sensitivity of protein NMR data, J. Am. Chem. Soc., 132, 2145–2147,
https://doi.org/10.1021/ja908004w, 2010.
Hyberts, S. G., Arthanari, H., Robson, S. A., and Wagner, G.: Perspectives in
magnetic resonance: NMR in the post-FFT era, J. Magn. Reson., 241,
60–73, https://doi.org/10.1016/j.jmr.2013.11.014, 2014.
Jameson, G., Hansen, A. L., Li, D., Bruschweiler-Li, L., and
Brüschweiler, R.: Extreme Nonuniform Sampling for Protein NMR Dynamics
Studies in Minimal Time, J. Am. Chem. Soc., 141, 16829–16838,
https://doi.org/10.1021/jacs.9b08032, 2019.
Juhlin, M., Elvander, F., Sward, J., and Jakobsson, A.: Fast Gridless
Estimation of Damped Modes, in: ISPACS 2018–2018 International Symposium on
Intelligent Signal Processing and Communication Systems, 27–30 November 2018, Okinawa, Japan, 346–351, 2018.
Kay, L. E., Nicholson, L. K., Delagio, F., Bax, A., and Torchia, D. A.: Pulse
sequences for removal of the effects of cross correlation between dipolar
and chemical-shift anisotropy relaxation mechanisms on the measurement of
heteronuclear T1 and T2 values in proteins, J. Magn. Reson., 97, 359–375,
1992a.
Kay, L. E., Keifer, P., and Saarinen, T.: Pure absorption gradient enhanced
heteronuclear single quantum correlation spectroscopy with improved
sensitivity, J. Am. Chem. Soc., 114, 10663–10665, 1992b.
Linnet, T. E. and Teilum, K.: Non-uniform sampling of NMR relaxation data,
J. Biomol. NMR, 64, 165–173, https://doi.org/10.1007/s10858-016-0020-6, 2016.
Mandel, A. M. and Palmer, A. G.: Measurement of relaxation rate constants
using constant-time accordion heteronuclear NMR spectroscopy, J. Magn.
Reson. Ser. A, 110, 62–72, 1994.
Månsson, A., Jakobsson, A., and Akke, M.: Multidimensional Cramér-Rao
lower bound for non-uniformly sampled NMR signals, in: European Signal
Processing Conference, 1–5 September 2014, Lisbon, Portugal, 974–978, 2014.
Massi, F., Johnson, E., Wang, C., Rance, M., and Palmer, A. G.: NMR R1
ρ
Rotating-Frame Relaxation with Weak Radio Frequency Fields, J. Am. Chem.
Soc., 126, 2247–2256, https://doi.org/10.1021/ja038721w, 2004.
Mayzel, M., Ahlner, A., Lundström, P., and Orekhov, V. Y.: Measurement of
protein backbone 13 CO and 15 N relaxation dispersion at high resolution, J.
Biomol. NMR, 69, 1–12, https://doi.org/10.1007/s10858-017-0127-4, 2017.
Mittermaier, A. K. and Kay, L. E.: Observing biological dynamics at atomic
resolution using NMR, Trends Biochem. Sci., 34, 601–611, https://doi.org/10.1016/j.tibs.2009.07.004, 2009.
Mobli, M. and Hoch, J. C.: Nonuniform sampling and non-Fourier signal
processing methods in multidimensional NMR, Prog. Nucl. Magn. Reson.
Spectrosc., 83, 21–41, https://doi.org/10.1016/j.pnmrs.2014.09.002, 2014.
Mulder, F. A. A., de Graaf, R. A., Kaptein, R., and Boelens, R.: An
off-resonance rotating frame relaxation experiment for the investigation of
macromolecular dynamics using adiabatic rotations, J. Magn. Reson., 131,
351–357, 1998.
Mulder, F. A. A., Skrynnikov, N. R., Hon, B., Dahlquist, F. W., and Kay, L.
E.: Measurement of slow (microseconds-milliseconds) time scale dynamics in
protein side chains by 15N relaxation dispersion NMR spectroscopy:
Application to Asn and Gln residues in a cavity mutant of T4 lysozyme, J.
Am. Chem. Soc., 123, 967–975, 2001.
Niklasson, M., Otten, R., Ahlner, A., Andresen, C., Schlagnitweit, J.,
Petzold, K., and Lundström, P.: Comprehensive analysis of NMR data using
advanced line shape fitting, J. Biomol. NMR, 69, 93–99,
https://doi.org/10.1007/s10858-017-0141-6, 2017.
Palmer, A. G.: NMR characterization of the dynamics of biomacromolecules,
Chem. Rev., 104, 3623–3640, https://doi.org/10.1021/cr030413t, 2004.
Palmer, A. G., Cavanagh, J., Wright, P. E., and Rance, M.: Sensitivity
improvement in proton-detected two-dimensional heteronuclear correlation NMR
spectroscopy, J. Magn. Reson., 93, 151–170, 1991.
Palmer, A. G., Skelton, N. J., Chazin, W. J., Wright, P. E., and Rance, M.:
Suppression of the effects of cross-correlation between dipolar and
anisotropic chemical shift relaxation mechanisms in the measurement of
spin-spin relaxation rates, Mol. Phys., 75, 699–711, 1992.
Press, W. H., Flannery, B. P., Teukolsky, S. A., and Vetterling, W. T.:
Numerical Recipes. The Art of Scientific Computing, Cambridge University
Press, Cambridge, UK, 1986.
Rabier, P., Kieffer, B., Koehl, P., and Lefevre, J.-F.: Fast measurement of
heteronuclear relaxation: frequency-domain analysis of NMR accordion
spectroscopy, Magn. Reson. Chem., 39, 447–456, 2001.
Skelton, N. J., Palmer, A. G., Akke, M., Kördel, J., Rance, M., and
Chazin, W. J.: Practical aspects of two-dimensional proton-detected 15N spin
relaxation measurements, J. Magn. Reson. Ser. B, 102, 253–264, 1993.
Stetz, M. A. and Wand, A. J.: Accurate determination of rates from
non-uniformly sampled relaxation data, J. Biomol. NMR, 65, 157–170,
https://doi.org/10.1007/s10858-016-0046-9, 2016.
Swärd, J., Adalbjörnsson, S. I., and Jakobsson, A.: High resolution
sparse estimation of exponentially decaying N-dimensional signals, Signal
Process., 128, 309–317, https://doi.org/10.1016/j.sigpro.2016.04.002, 2016.
Urbańczyk, M., Nowakowski, M., Koźmiński, W., and Kazimierczuk,
K.: Joint non-uniform sampling of all incremented time delays for quicker
acquisition in protein relaxation studies, J. Biomol. NMR, 68, 155–161,
https://doi.org/10.1007/s10858-017-0115-8, 2017.
Wallerstein, J., Misini Ignjatovic, M., Kumar, R., Caldararu, O., Peterson, K., Leffler, H., Logan, D., Nilsson, U., Ryde, U., and Akke, M.: Entropy-Entropy Compensation Between the Conformational and Solvent Degrees of Freedom Fine-tunes Affinity in Ligand Binding to Galectin-3C, Biological Magnetic Resonance Data Bank, https://doi.org/10.13018/BMR50283, 2020.
Wallerstein, J., Ekberg, V., Misini Ignjatović, M., Kumar, R.,
Caldararu, O., Peterson, K., Leffler, H., Logan, D. T., Nilsson, U. J.,
Ryde, U., and Akke, M.: Entropy–Entropy Compensation Between the
Conformational and Solvent Degrees of Freedom Fine-tunes Affinity in Ligand
Binding to Galectin-3C, JACS Au, 1, 484–500, https://doi.org/10.1021/jacsau.0c00094,
2021.
Wang, A. C. and Bax, A.: Minimizing the effects of radio-frequency heating
in multidimensional NMR experiments, J. Biomol. NMR, 3, 715–720, 1993.
Waudby, C. A., Burridge, C., and Christodoulou, J.: Optimal design of
adaptively sampled NMR experiments for measurement of methyl group dynamics
with application to a ribosome-nascent chain complex, J. Magn. Reson., 326,
106937, https://doi.org/10.1016/j.jmr.2021.106937, 2021.
Wernersson, S., Carlström, G., Jakobsson, A., and Akke, M.: Data for: Rapid measurement of heteronuclear transverse relaxation rates using non-uniformly sampled R1rho accordion experiments, Mendeley Data, V1 [data set], https://doi.org/10.17632/zyryxrgkc3.1, 2021.
Yip, G. N. B. and Zuiderweg, E. R. P.: A phase cycle scheme that
significantly suppresses offset-dependent artifacts in the R-2-CPMG N-15
relaxation experiment, J. Magn. Reson., 171, 25–36, 2004.
