Equbal, A., Shankar, R., Leskes, M., Vega, S. S. S. S.
, Nielsen, N. C. & Madhu, P. K. (2017).
Significance of symmetry in the nuclear spin Hamiltonian for efficient heteronuclear dipolar decoupling in solid-state NMR: A Floquet description of supercycled rCW schemes.
Journal of Chemical Physics,
146(10), Article 104202.
https://doi.org/10.1063/1.4977738
Goswami, M., Madhu, P. K.
, Dittmer, J., Nielsen, N. C. & Ganapathy, S. (2009).
Sensitivity enhancement of 29Si double-quantum dipolar recoupling spectroscopy by Carr-Purcell-Meiboom-Gill acquisition method.
Chemical Physics Letters,
478, 287-291.
Larsen, F. H.
, Jakobsen, H. J., Ellis, P. D.
& Nielsen, N. C. (1997).
Sensitivity-Enhanced Quadrupolar-Echo NMR of Half-Integer Quadrupolar Nuclei. Magnitudes and Relative Orientation of Chemical Shielding and Quadrupolar Coupling Tensors.
Journal of Physical Chemistry Part A: Molecules, Spectroscopy, Kinetics, Environment and General Theory,
101, 8597-8606.
Vosegaard, T., Larsen, F. H.
, Jakobsen, H. J., Ellis, P. D.
& Nielsen, N. C. (1997).
Sensitivity-Enhanced Multiple-Quantum MAS NMR of Half-Integer Quadrupolar Nuclei.
Journal of the American Chemical Society,
119, 9055-9056.
Weber, M., Schneider, D., Prodöhl, A., Dreher, C., Becker, C.
, Underhaug, J., Svane, A. S. P., Malmendal, A., Nielsen, N. C. & Otzen, D. (2011).
SDS-facilitated in vitro formation of a transmembrane B-type cytochrome is mediated by changes in local pH.
Journal of Molecular Biology,
407(4), 594-606.
https://doi.org/10.1016/j.jmb.2011.02.005
Kalashnyk, N., Nielsen, J. T., Nielsen, E. H., Skrydstrup, T., Otzen, D., Lægsgaard, E., Wang, C.
, Besenbacher, F., Nielsen, N. C. & Linderoth, T. R. (2012).
Scanning tunneling microscopy reveals single-molecule insights into the self-assembly of amyloid fibrils.
A C S Nano,
6(8), 6882-6889.
https://doi.org/10.1021/nn301708d
Equbal, A., Paul, S., Mithu, V. S.
, Vinther, J. M., Nielsen, N. C. & Madhu, P. K. (2014).
rTPPM: Towards Improving Solid-State NMR Two-Pulse Phase-Modulation Heteronuclear Dipolar Decoupling Sequence by Refocusing.
Journal of Magnetic Resonance,
244, 68-73.
https://doi.org/10.1016/j.jmr.2014.04.009
Vosegaard, T., Bertelsen, K., Pedersen, J. M., Thøgersen, L., Schiøtt, B., Tajkhorshid, E.
, Skrydstrup, T. & Nielsen, N. C. (2008).
Resolution Enhancement in Solid-State NMR of Oriented Membrane Proteins by Anisotropic Differential Linebroadening.
Journal of the American Chemical Society,
130, 5028-5029.
Bertelsen, K., Jensen, B. P., Thøgersen, L., Tajkhorshid, E.
, Schiøtt, H. B., Skrydstrup, T., Nielsen, N. C. & Vosegaard, T. (2009).
Residue-Specific Information about the Dynamics of Antimicrobial Peptides from 1H−15N and 2H Solid-State NMR Spectroscopy.
Journal of the American Chemical Society,
131(51), 18335–18342.
https://doi.org/10.1021/ja908604u
Bundgaard, E., Hagemann, O.
, Bjerring, M., Nielsen, N. C., Andreasen, J. W., Andreasen, B. & Krebs, F. C. (2012).
Removal of Solubilizing Side Chains at Low Temperature: A New Route to Native Poly(thiophene).
Macromolecules,
45(8), 3644-3646.
https://doi.org/10.1021/ma300075x
Equbal, A., Leskes, M.
, Nielsen, N. C., Madhu, P. K. & Vega, S. S. S. S. (2016).
Relative merits of rCWA and XiX heteronuclear spin decoupling in solid-state magic-angle-spinning NMR spectroscopy: A bimodal Floquet analysis.
Journal of Magnetic Resonance,
263, 55-64.
https://doi.org/10.1016/j.jmr.2015.12.019
Vinther, J. M., Nielsen, A. B.
, Bjerring, M., van Eck, E., Kentgens, A., Khaneja, N.
& Nielsen, N. C. (2012).
Refocused continuous-wave decoupling: A new approach to heteronuclear dipolar decoupling in solid-state NMR spectroscopy.
Journal of Chemical Physics,
137(21), 214202.
https://doi.org/10.1063/1.4768953
Maximov, I. I.
, Vinding, M. S., Tse, D. H. Y.
, Nielsen, N. C. & Shah, N. J. (2015).
Real-time 2D spatially selective MRI experiments: Comparative analysis of optimal control design methods.
Journal of Magnetic Resonance,
254(110-120), 110-120.
https://doi.org/10.1016/j.jmr.2015.03.003
Bjerring, M. M., Jensen, B. P., Oschkinat, H. H.
, Akbey, U. & Nielsen, N. C. (2012).
Rapid solid-state NMR of deuterated proteins by interleaved cross-polarization from 1 H and 2 H nuclei.
Journal of Magnetic Resonance,
214, 324-328.
https://doi.org/10.1016/j.jmr.2011.10.020
Akbey, Ü., Nieuwkoop, A. J., Wegner, S., Voreck, A., Kunert, B., Bandara, P., Engelke, F.
, Nielsen, N. C. & Oschkinat, H. (2014).
Quadruple-resonance magic-angle spinning NMR spectroscopy of deuterated solid proteins.
Angewandte Chemie,
53(9), 2438-42.
https://doi.org/10.1002/anie.201308927
Runager, K., Garcia-Castellanos, R.
, Valnickova, Z., Kristensen, T., Nielsen, N. C., Klintworth, G. K., Gomis-Ruth, F. X.
& Enghild, J. J. (2009).
Purification, crystallization and preliminary X-raydiffraction of wild-type and mutant recombinanthuman transforming growth factor b-inducedprotein (TGFBIp).
Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online,
65, 299-303.
Kosicka, I., Kristensen, T., Bjerring, M., Thomsen, K., Scavenius, C., Enghild, J. J. & Nielsen, N. C. (2014).
Preparation of Uniformly 13C,15N-Labeled Recombinant Human Amylin for Solid-State NMR Investigation.
Protein Expression and Purification,
99, 119-130.
https://doi.org/10.1016/j.pep.2014.04.002
Ghodke, S. D., Jensen, G. V., Svane, A. S. P., Weise, K.
, Søndergaard, A., Behrens, M. A., Pedersen, J. S., Nielsen, N. C., Pedersen, J. S., Winter, R.
& Otzen, D. (2014).
Polymorphism, metastable species and interconversion: the many states of glucagon fibrils. In V. Uversky & Y. Lyubchenko (Eds.),
Bio-nanoimaging: Protein misfolding and aggregation (pp. 373-386). Elsevier.
https://doi.org/10.1016/B978-0-12-394431-3.00034-1
Andreasen, M., Nielsen, S. B., Runager, K., Christiansen, G., Nielsen, N. C., Enghild, J. J. & Otzen, D. (2012).
Polymorphic Fibrillation of the Destabilized Fourth Fasciclin-1 Domain Mutant A546T of the Transforming Growth Factor-β-induced Protein (TGFBIp) Occurs through Multiple Pathways with Different Oligomeric Intermediates.
Journal of Biological Chemistry,
287(41), 34730-34742.
https://doi.org/10.1074/jbc.M112.379552
Vu-Quang, H., Vinding, M. S., Nielsen, T., Ullisch, M. G., Nielsen, N. C., Nguyen, D. T.
& Kjems, J. (2019).
Pluronic F127-folate coated super paramagenic iron oxide nanoparticles as contrast agent for cancer diagnosis in magnetic resonance imaging.
Polymers,
11(4), Article 743.
https://doi.org/10.3390/polym11040743
Thøgersen, L., Schiøtt, B., Vosegaard, T., Nielsen, N. C. & Tajkhorshid, E. (2008).
Peptide Aggregation and Pore Formation in a Lipid Bilayer: A Combined Coarse-Grained and All Atom Molecular Dynamics Study.
Biophysical Journal,
95(9), 4337-4347.
https://doi.org/10.1529/biophysj.108.133330
Vad, B. S., Bertelsen, K., Johansen, C. H.
, Pedersen, J. M., Skrydstrup, T., Nielsen, N. C. & Otzen, D. E. (2010).
Pardaxin permeabilizes vesicles more efficiently by pore formation than by disruption.
Biophysical Journal,
98(4), 576-85.
https://doi.org/10.1016/j.bpj.2009.08.063
Equbal, A., Madhu, P. K., Meier, B. H.
, Nielsen, N. C., Ernst, M. & Agarwal, V. (2017).
Parameter independent low-power heteronuclear decoupling for fast magic-angle spinning solid-state NMR.
Journal of Chemical Physics,
146(8), Article 139901.
https://doi.org/10.1063/1.4979997,
https://doi.org/10.1063/1.4976997
Untidt, T., Schulte-Herbrüggen, T., Sørensen, O. W.
& Nielsen, N. C. (1999).
Optimum α/β-HSQC pulse sequences for coherence-order-; spin-state-selective transfer in I2S spin systems.
Journal of Physical Chemistry Part A: Molecules, Spectroscopy, Kinetics, Environment and General Theory,
103, 8921-8926.
Oktaviani, N. A.
, Risør, M. W., Lee, Y-H., Megens, R. P., de Jong, D. H., Otten, R., Scheek, R. M.
, Enghild, J. J., Nielsen, N. C., Ikegami, T.
& Mulder, F. A. A. (2015).
Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide.
Journal of Biomolecular N M R,
62(2), 129-142.
https://doi.org/10.1007/s10858-015-9925-8
Vinding, M. S., Maximov, I., Tosner, Z., Jespersen, S. N. & Nielsen, N. C. (2011).
Optimal Control Theory in Magnetic Resonance Imaging: Global Optima for 2DRF pulses. Poster session presented at 32nd Annual Danish NMR Meeting, Korsør, Denmark.
Laustsen, C., Bowen, S.
, Vinding, M. S., Nielsen, N. C. & Ardenkjær-Larsen, J. H. (2013).
OPTIMAL CONTROL SINGLET STATE STORAGE FOR CLINICAL MR SYSTEMS. Abstract from ISMRM 2013, Salt Lake City, United States.
Tosner, Z., Vosegaard, T., Kehlet, C., Khaneja, N., Glaser, S.
& Nielsen, N. C. (2009).
Optimal control in NMR spectroscopy: Numerical implementation in SIMPSON.
Journal of Magnetic Resonance,
197, 120-134.
https://doi.org/10.1016/j.jmr.2008.11.020
Kehlet, C., Tosner, Z., Nielsen, A. B., Bjerring, M., Nielsen, J. T., Vinding, M. S., Vosegaard, T., Glaser, S. J., Khaneja, N.
& Nielsen, N. C. (2009).
Optimal Control in NMR Spectroscopy: Implementation into SIMPSON and Novel Experiments for Biological Solid-State NMR. Poster session presented at 50th Experimental NMR Conference (ENC), Asilomar, CA, United States.
Kehlet, C., Bjerring, M., Sivertsen, A. C., Kristensen, T., Enghild, J. J., Glaser, S. J., Khaneja, N.
& Nielsen, N. C. (2007).
Optimal control based NCO and NCA experiments for spectral assignment in biological solid-state NMR spectroscopy.
Journal of Magnetic Resonance,
188(2), 216-230.
https://doi.org/10.1016/j.jmr.2007.06.011
Hansen, J. Ø., Kehlet, C.
, Bjerring, M., Vosegaard, T., Glaser, S., Khaneja, N.
& Nielsen, N. C. (2007).
Optimal control based design of composite dipolar recoupling experiments by analogy to single-spin inversion pulses.
Chemical Physics Letters,
447, 154-161.
https://doi.org/10.1016/j.cplett.2007.08.072
Wei, D., Akbey, U.
, Jensen, B. P., Oschkinat, H., Reif, B.
, Bjerring, M. & Nielsen, N. C. (2011).
Optimal 2H rf pulses and 2H-13C cross-polarization methods for solid-state 2H MAS NMR of perdeuterated proteins.
The Journal of Physical Chemistry Letters,
2(11), 1289-1294.
https://doi.org/10.1021/jz200511b
Sørensen, M. K., Balsgart, N. M., Beyer, M., Jensen, O. N.
& Nielsen, N. C. (2022).
On-Site Measurement of Fat and Protein Contents in Milk Using Mobile NMR Technology.
Molecules,
27(3), Article 583.
https://doi.org/10.3390/molecules27030583