Find

For students
For PhDs
For employees

Interdisciplinary Nanoscience Center

Danish Center for Ultrahigh Field NMR Spectroscopy

Publications

Sort by: Date | Author | Title

Møller, K. V., Nguyen, H. T. T., Mørch, M. G. M., Hesselager, M. O., Mulder, F. A. A., Fuursted, K. & Olsen, A. (2022). A Lactobacilli diet that confers MRSA resistance causes amino acid depletion and increased antioxidant levels in the C. elegans host. Frontiers in Microbiology, 13, [886206]. https://doi.org/10.3389/fmicb.2022.886206

Hoffmann, F., Mulder, F. A. A. & Schäfer, L. V. (2022). How Much Entropy Is Contained in NMR Relaxation Parameters? Journal of Physical Chemistry B, 126(1), 54-68. https://doi.org/10.1021/acs.jpcb.1c07786

Ali, A. A. A. I., Hoffmann, F., Schäfer, L. V. & Mulder, F. A. . A. (2022). Probing Methyl Group Dynamics in Proteins by NMR Cross-Correlated Dipolar Relaxation and Molecular Dynamics Simulations. Journal of Chemical Theory and Computation, 18(12), 7722-7732. https://doi.org/10.1021/acs.jctc.2c00568

Stødkilde, K., Nielsen, J. T., Petersen, S. V., Paetzold, B., Brüggemann, H., Mulder, F. A. A. & Andersen, C. B. F. (2022). Solution Structure of the Cutibacterium acnes-Specific Protein RoxP and Insights Into Its Antioxidant Activity. Frontiers in cellular and infection microbiology, 12, [803004]. https://doi.org/10.3389/fcimb.2022.803004

Lenard, A. J., Mulder, F. A. A. & Madl, T. (2022). Solvent paramagnetic relaxation enhancement as a versatile method for studying structure and dynamics of biomolecular systems. Progress in Nuclear Magnetic Resonance Spectroscopy, 132-133, 113-139. https://doi.org/10.1016/j.pnmrs.2022.09.001

Hansen, A. R. E., Enemark-Rasmussen, K., Mulder, F. A. A., Jensen, P. R. & Meier, S. (2022). Versatile Procedures for Reliable NMR Quantification of CO2 Electroreduction Products. Journal of Physical Chemistry C, 126(27), 11026-11032. https://doi.org/10.1021/acs.jpcc.2c03448

Nielsen, J. T. & Mulder, F. A. A. (2021). CheSPI: chemical shift secondary structure population inference. Journal of Biomolecular NMR, 75(6-7), 273-291. https://doi.org/10.1007/s10858-021-00374-w

Andersen, C. B., Yoshimura, Y., Nielsen, J., Otzen, D. E. & Mulder, F. A. A. (2021). How epigallocatechin gallate binds and assembles oligomeric forms of human alpha-synuclein. The Journal of Biological Chemistry, 296, [100788]. https://doi.org/10.1016/j.jbc.2021.100788

Andersen, C., Grønnemose, A. L., Pedersen, J. N., Nowak, J. S., Christiansen, G., Nielsen, J., Mulder, F. A. A., Otzen, D. E. & Jørgensen, T. J. D. (2021). Lipid Peroxidation Products HNE and ONE Promote and Stabilize Alpha-Synuclein Oligomers by Chemical Modifications. Biochemistry, 60(47), 3644-3658. https://doi.org/10.1021/acs.biochem.1c00478

Mulder, F. A. A. (2021). NMR spectroscopy charges into protein surface electrostatics. Proceedings of the National Academy of Sciences, 118(30), [2110176118]. https://doi.org/10.1073/pnas.2110176118

Dass, R., Corlianò, E. & Mulder, F. A. A. (2021). The contribution of electrostatics to hydrogen exchange in the unfolded protein state. Biophysical Journal, 120(18), 4107-4114. https://doi.org/10.1016/j.bpj.2021.08.003

Guo, X., Sarup, P. M., Jensen, J. D., Jihad, O., Kristensen, N. H., Mulder, F. A. A., Jahoor, A. & Jensen, J. (2020). Genetic Variance of Metabolomic Features and Their Relationship With Malting Quality Traits in Spring Barley. Frontiers in Plant Science, 11, [575467]. https://doi.org/10.3389/fpls.2020.575467

Dass, R., Mulder, F. A. A. & Nielsen, J. T. (2020). ODiNPred: comprehensive prediction of protein order and disorder. Scientific Reports, 10(1), [14780]. https://doi.org/10.1038/s41598-020-71716-1

Dass, R. & Mulder, F. A. A. (2020). Paris-DÉCOR: A Protocol for the Determination of Fast Protein Backbone Amide Hydrogen Exchange Rates. In B. B. Kragelund & K. Skriver (Eds.), Intrinsically Disordered Proteins (pp. 337-344). Humana Press. Methods in Molecular Biology Vol. 2141 https://doi.org/10.1007/978-1-0716-0524-0_17

Hoffmann, F., Mulder, F. A. A. & Schäfer, L. V. (2020). Predicting NMR relaxation of proteins from molecular dynamics simulations with accurate methyl rotation barriers. Journal of Chemical Physics, 152(8), [084102]. https://doi.org/10.1063/1.5135379

Nielsen, J. T. & Mulder, F. A. A. (2020). Quantitative Protein Disorder Assessment Using NMR Chemical Shifts. In B. B. Kragelund & K. Skriver (Eds.), Intrinsically Disordered Proteins (pp. 303-317). Humana Press. Methods in Molecular Biology Vol. 2141 https://doi.org/10.1007/978-1-0716-0524-0_15

Yoshimura, Y. & Mulder, F. A. A. (2020). Sensitive and simplified: a combinatorial acquisition of five distinct 2D constant-time ¹³C− ¹H NMR protein correlation spectra. Journal of Biomolecular NMR, 74(12), 695-706. https://doi.org/10.1007/s10858-020-00341-x

Hansen, B. K., Larsen, C. K., Nielsen, J. T., Svenningsen, E. B., Van, L. B., Jacobsen, K. M., Bjerring, M., Flygaard, R. K., Jenner, L. B., Nejsum, L. N., Brodersen, D. E., Mulder, F. A. A., Tørring, T. & Poulsen, T. B. (2020). Structure and Function of the Bacterial Protein Toxin Phenomycin. Structure, 28(5), 528-539.e9. https://doi.org/10.1016/j.str.2020.03.003

Mulder, F. A. A., Tenori, L. & Luchinat, C. (2019). Fast and Quantitative NMR Metabolite Analysis Afforded by a Paramagnetic Co-Solute. Angewandte Chemie - International Edition, 58(43), 15283-15286. https://doi.org/10.1002/anie.201908006

Xue, M., Wakamoto, T., Kejlberg, C., Yoshimura, Y., Nielsen, T. A., Risør, M. W., Sanggaard, K. W., Kitahara, R. & Mulder, F. A. A. (2019). How internal cavities destabilize a protein. Proceedings of the National Academy of Sciences, 116(42), 21031-21036. https://doi.org/10.1073/pnas.1911181116

Dass, R., Corlianò, E. & Mulder, F. A. A. (2019). Measurement of Very Fast Exchange Rates of Individual Amide Protons in Proteins by NMR Spectroscopy. ChemPhysChem, 20(2), 231-235. https://doi.org/10.1002/cphc.201801044

Nielsen, J. T. & Mulder, F. A. A. (2019). Quality and bias of protein disorder predictors. Scientific Reports, 9, [5137]. https://doi.org/10.1038/s41598-019-41644-w

Hoffmann, F., Mulder, F. A. A. & Schaefer, L. V. (2018). Accurate Methyl Group Dynamics in Protein Simulations with AMBER Force Fields. Journal of Physical Chemistry B, 122(19), 5038-5048. https://doi.org/10.1021/acs.jpcb.8b02769

Mulder, F. A. A. (2018). Fuzzy and fast nuclear transport. Journal of Biological Chemistry, 293(12), 4564-4565. https://doi.org/10.1074/jbc.H118.002129

Hoffmann, F., Xue, M., Schäfer, L. V. & Mulder, F. A. A. (2018). Narrowing the gap between experimental and computational determination of methyl group dynamics in proteins. Physical Chemistry Chemical Physics, 20(38), 24577-24590. https://doi.org/10.1039/c8cp03915a

Kitahara, R., Sakuraba, S., Kameda, T., Okuda, S., Xue, M. & Mulder, F. A. A. (2018). Nuclear magnetic resonance-based determination of dioxygen binding sites in protein cavities. Protein Science, 27(3), 769-779. https://doi.org/10.1002/pro.3371

Nielsen, J. T. & Mulder, F. A. A. (2018). POTENCI: prediction of temperature, neighbor and pH-corrected chemical shifts for intrinsically disordered proteins. Journal of Biomolecular NMR, 70(3), 141-165. https://doi.org/10.1007/s10858-018-0166-5

Tamiola, K., Scheek, R. M., Van Der Meulen, P. & Mulder, F. A. A. (2018). PepKalc: Scalable and comprehensive calculation of electrostatic interactions in random coil polypeptides. Bioinformatics, 34(12), 2053-2060. https://doi.org/10.1093/bioinformatics/bty033

Kurnik, M., Sahin, C., Andersen, C. B., Lorenzen, N., Giehm, L., Mohammad-Beigi, H., Jessen, C. M., Pedersen, J. S., Christiansen, G., Petersen, S. V., Staal, R., Krishnamurthy, G., Pitts, K., Reinhart, P. H., Mulder, F. A. A., Mente, S., Hirst, W. D. & Otzen, D. E. (2018). Potent α-Synuclein Aggregation Inhibitors, Identified by High-Throughput Screening, Mainly Target the Monomeric State. Cell Chemical Biology, 25(11), 1389-1402. https://doi.org/10.1016/j.chembiol.2018.08.005

Madl, T. & Mulder, F. A. A. (2018). Small Paramagnetic Co-solute Molecules. In C. Luchinat, G. Parigi & E. Ravera (Eds.), Paramagnetism in Experimental Biomolecular NMR (Vol. 2018/16, pp. 283-309). Royal Society of Chemistry. New Developments in NMR https://doi.org/10.1039/9781788013291-00283

Oktaviani, N. A., Pool, T. J., Yoshimura, Y., Kamikubo, H., Scheek, R. M., Kataoka, M. & Mulder, F. A. A. (2017). Active-Site pKa Determination for Photoactive Yellow Protein Rationalizes Slow Ground-State Recovery. Biophysical Journal, 112(10), 2109-2116. https://doi.org/10.1016/j.bpj.2017.04.008

Yoshimura, Y., Holmberg, M., Kukic, P., Andersen, C. B., Mata-Cabana, A., Falsone, S. F., Vendruscolo, M., Nollen, E. A. A. & Mulder, F. (2017). MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions. Journal of Biological Chemistry, 292(20), 8269-8278. https://doi.org/10.1074/jbc.M116.764886

Yoshimura, Y., Oktaviani, N. A., Yonezawa, K., Kamikubo, H. & Mulder, F. A. A. (2017). Unambiguous Determination of Protein Arginine Ionization States in Solution by NMR Spectroscopy. Angewandte Chemie International Edition, 56(1), 239–242. https://doi.org/10.1002/anie.201609605

Xue, M., Kitahara, R., Yoshimura, Y. & Mulder, F. A. A. (2016). Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation. Biochemical and Biophysical Research Communications, 478(3), 1185-1188. https://doi.org/10.1016/j.bbrc.2016.08.092

Kitahara, R., Yoshimura, Y., Xue, M., Kameda, T. & Mulder, F. A. A. (2016). Detecting O₂ binding sites in protein cavities. Scientific Reports, 6, [20534]. https://doi.org/10.1038/srep20534

Kulminskaya, N. V., Yoshimura, Y., Runager, K., Sørensen, C. S., Bjerring, M., Andreasen, M., Otzen, D. E., Enghild, J. J., Nielsen, N. C. & Mulder, F. A. A. (2016). Near-complete ¹H, ¹³C, ¹⁵N resonance assignments of dimethylsulfoxide-denatured TGFBIp FAS1-4 A546T. Biomolecular N M R Assignments, 10(1), 25-29. https://doi.org/10.1007/s12104-015-9630-2

Nielsen, J. T. & Mulder, F. A. A. (2016). There is Diversity in Disorder-"In all Chaos there is a Cosmos, in all Disorder a Secret Order". Frontiers in Molecular Biosciences, 3, [4]. https://doi.org/10.3389/fmolb.2016.00004

Maeno, A., Sindhikara, D., Hirata, F., Otten, R., Dahlquist, F. W., Yokoyama, S., Akasaka, K., Mulder, F. A. A. & Kitahara, R. (2015). Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme. Biophysical Journal, 108(1), 133-45. https://doi.org/10.1016/j.bpj.2014.11.012

Hass, M. A. S. & Mulder, F. A. A. (2015). Contemporary NMR Studies of Protein Electrostatics. Annual Review of Biophysics, 44, 53-75. https://doi.org/10.1146/annurev-biophys-083012-130351

Yoshimura, Y., Kulminskaya, N. V. & Mulder, F. A. A. (2015). Easy and unambiguous sequential assignments of intrinsically disordered proteins by correlating the backbone (15)N or (13)C' chemical shifts of multiple contiguous residues in highly resolved 3D spectra. Journal of Biomolecular N M R, 61(2), 109-121. https://doi.org/10.1007/s10858-014-9890-7

Kitahara, R. & Mulder, F. A. A. (2015). Is pressure-induced signal loss in NMR spectra for the Leu99Ala cavity mutant of T₄ lysozyme due to unfolding? Proceedings of the National Academy of Sciences, 112(9), [E923]. https://doi.org/10.1073/pnas.1423279112

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

Olesen, H. G., Mohr, D., Seweryn, P., Yoshimura, Y., Kutlubaeva, Z., Dolman, F., Chelchessa, B., Chetverin, A. B., Mulder, F. A. A., Brodersen, D. E. & Knudsen, C. R. (2015). Structural basis for RNA-genome recognition during bacteriophage Qβ replication. Nucleic Acids Research, 43(22), 10893-10906. https://doi.org/10.1093/nar/gkv1212

Hong, Z., Nowakowski, M., Spronk, C., Petersen, S. V., Andreasen, P., Koźmiński, W., Mulder, F. & Jensen, J. K. (2015). The solution structure of the MANEC-type domain from Hepatocyte Growth Factor Activator Inhibitor 1 reveals an unexpected PAN/apple domain-type fold. Biochemical Journal, 466(2), 299-309. https://doi.org/10.1042/BJ20141236

O'Malley, T. T., Oktaviani, N. A., Zhang, D., Lomakin, A., O'Nuallain, B., Linse, S., Benedek, G. B., Rowan, M. J., Mulder, F. A. A. & Walsh, D. M. (2014). Aβ dimers differ from monomers in structural propensity, aggregation paths and population of synaptotoxic assemblies. Biochemical Journal, 461(3), 413-426. https://doi.org/10.1042/BJ20140219

Lorenzen, N., Nielsen, S. B., Yoshimura, Y., Vad, B. S., Andersen, C. B., Betzer, C., Kaspersen, J. D., Christiansen, G., Pedersen, J. S., Jensen, P. H., Mulder, F. A. A. & Otzen, D. E. (2014). How epigallocatechin gallate can inhibit α-synuclein oligomer toxicity in vitro. Journal of Biological Chemistry, 289(31), 21299-21310. https://doi.org/10.1074/jbc.M114.554667

Chu, B. C. H., Otten, R., Krewulak, K. D., Mulder, F. A. A. & Vogel, H. J. (2014). The Solution Structure, Binding Properties, and Dynamics of the Bacterial Siderophore-binding Protein FepB. Journal of Biological Chemistry, 289(42), 29219-29234. https://doi.org/10.1074/jbc.M114.564021

Pool, T. J., Oktaviani, N. A., Kamikubo, H., Kataoka, M. & Mulder, F. A. A. (2013). ¹H, ¹³C, and ¹⁵N resonance assignment of photoactive yellow protein. Biomolecular N M R Assignments, 7(1), 97-100. https://doi.org/10.1007/s12104-012-9387-9

Avanti, C., Oktaviani, N. A., Hinrichs, W. L. J., Frijlink, H. W. & Mulder, F. A. A. (2013). Aspartate buffer and divalent metal ions affect oxytocin in aqueous solution and protect it from degradation. International Journal of Pharmaceutics, 444(1-2), 139-145. https://doi.org/10.1016/j.ijpharm.2013.01.051

Roodbeen, R., Paaske, B., Jiang, L., Jensen, J. K., Christensen, A., Nielsen, J. T., Huang, M., Mulder, F. A. A., Nielsen, N. C., Andreasen, P. & Jensen, K. J. (2013). Bicyclic Peptide Inhibitor of Urokinase-Type Plasminogen Activator: Mode of Action. ChemBioChem, 14(16), 2179–2188. https://doi.org/10.1002/cbic.201300335

Displaying results 1 to 50 out of 100

1

Revised 17.04.2023

-

Lise Refstrup Linnebjerg Pedersen