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Interdisciplinary Nanoscience Center

Danish Center for Ultrahigh Field NMR Spectroscopy

Publications

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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

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

Wood, K., Gallat, F.-X., Otten, R., van Heel, A. J., Lethier, M., van Eijck, L., Moulin, M., Haertlein, M., Weik, M. & Mulder, F. A. A. (2013). Protein Surface and Core Dynamics Show Concerted Hydration-Dependent Activation. Angewandte Chemie International Edition, 52(2), 665-668. https://doi.org/10.1002/anie.201205898

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

Wood, K., Paz, A., Dijkstra, K., Scheek, R. M., Otten, R., Silman, I., Sussman, J. L. & Mulder, F. A. A. (2012). Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3. Biomolecular N M R Assignments, 6(1), 15-8. https://doi.org/10.1007/s12104-011-9315-4

Oktaviani, N. A., Pool, T. J., Kamikubo, H., Slager, J., Scheek, R. M., Kataoka, M. & Mulder, F. A. A. (2012). Comprehensive determination of protein tyrosine pKa values for photoactive yellow protein using indirect 13C NMR spectroscopy. Biophysical Journal, 102(3), 579-86. https://doi.org/10.1016/j.bpj.2011.12.024

Mulder, F. A. A. & Scheek, R. M. (2012). Multidimensional NMR spectroscopy. In G. C. K. Roberts (Ed.), Encyclopedia of Biophysics Springer.

Tamiola, K. & Mulder, F. A. A. (2012). Using NMR chemical shifts to calculate the propensity for structural order and disorder in proteins. Biochemical Society. Transactions, 40(5), 1014-20. https://doi.org/10.1042/BST20120171

Oktaviani, N. A., Otten, R., Dijkstra, K., Scheek, R. M., Thulin, E., Akke, M. & Mulder, F. A. A. (2011). 100% complete assignment of non-labile (1)H, (13)C, and (15)N signals for calcium-loaded Calbindin D(9k) P43G. Biomolecular N M R Assignments, 5(1), 79-84. https://doi.org/10.1007/s12104-010-9272-3

Gardner, K. H., Mittermaier, A. & Mulder, F. A. A. (2011). A tribute to Lewis E Kay on his 50th birthday. Journal of Biomolecular N M R, 51(1-2), 51: pp 3-4. https://doi.org/10.1007/s10858-011-9561-x

Karasawa, A., Erkens, G. B., Berntsson, R. P.-A., Otten, R., Schuurman-Wolters, G. K., Mulder, F. A. A. & Poolman, B. (2011). Cystathionine β-synthase (CBS) domains 1 and 2 fulfill different roles in ionic strength sensing of the ATP-binding cassette (ABC) transporter OpuA. Journal of Biological Chemistry, 286(43), 37280-91. https://doi.org/10.1074/jbc.M111.284059

Meinema, A. C., Laba, J. K., Hapsari, R. A., Otten, R., Mulder, F. A. A., Kralt, A., van den Bogaart, G., Lusk, C. P., Poolman, B. & Veenhoff, L. M. (2011). Long unfolded linkers facilitate membrane protein import through the nuclear pore complex. Science, 333(6038), 90-3. https://doi.org/10.1126/science.1205741

Tamiola, K. & Mulder, F. A. A. (2011). ncIDP-assign: a SPARKY extension for the effective NMR assignment of intrinsically disordered proteins. Bioinformatics (Online), 27(7), 1039-40. https://doi.org/10.1093/bioinformatics/btr054

Mulder, F. A. A., Otten, R. & Scheek, R. M. (2011). Origin and removal of mixed-phase artifacts in gradient sensitivity enhanced heteronuclear single quantum correlation spectra. Journal of Biomolecular N M R, 51(1-2), 199-207. https://doi.org/10.1007/s10858-011-9554-9

Otten, R., Chu, B., Krewulak, K. D., Vogel, H. J. & Mulder, F. A. A. (2010). Comprehensive and cost-effective NMR spectroscopy of methyl groups in large proteins. Journal of the American Chemical Society, 132(9), 2952-2960. https://doi.org/10.1021/ja907706a

Hansen, D. F., Neudecker, P., Vallurupalli, P., Mulder, F. A. A. & Kay, L. E. (2010). Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion. Journal of the American Chemical Society, 132(1), 42-43. https://doi.org/10.1021/ja909294n

Mulder, F. A. A. & Filatov, M. (2010). NMR chemical shift data and ab initio shielding calculations: Emerging tools for protein structure determination. Chemical Society Reviews, 39(2), 578-590. https://doi.org/10.1039/b811366c

Lindman, S., Bauer, M. C., Lund, M., Diehl, C., Mulder, F. A. A., Akke, M. & Linse, S. (2010). PK_a values for the unfolded state under native conditions explain the pH-dependent stability of PGB1. Biophysical Journal, 99(10), 3365-3373. https://doi.org/10.1016/j.bpj.2010.08.078

Otten, R., Villali, J., Kern, D. & Mulder, F. A. A. (2010). Probing microsecond time scale dynamics in proteins by methyl ¹H Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC^r. Journal of the American Chemical Society, 132(47), 17004-17014. https://doi.org/10.1021/ja107410x

Tamiola, K., Acar, B. & Mulder, F. A. A. (2010). Sequence-specific random coil chemical shifts of intrinsically disordered proteins. Journal of the American Chemical Society, 132(51), 18000-3. https://doi.org/10.1021/ja105656t

Wood, K., Tobias, D. J., Kessler, B., Gabel, F., Oesterhelt, D., Mulder, F. A. A., Zaccai, G. & Weik, M. (2010). The low-temperature inflection observed in neutron scattering measurements of proteins is due to methyl rotation: Direct evidence using isotope labeling and molecular dynamics simulations. Journal of the American Chemical Society, 132(14), 4990-4991. https://doi.org/10.1021/ja910502g

Otten, R., Wood, K. & Mulder, F. A. A. (2009). Comprehensive determination of ³J_HNHα for unfolded proteins using ¹³C′-resolved spin-echo difference spectroscopy. Journal of Biomolecular N M R, 45(4), 343-349. https://doi.org/10.1007/s10858-009-9382-3

Paz, A., Zeev-Ben-Mordehai, T., Lundqvist, M., Sherman, E., Mylonas, E., Weiner, K. L., Haran, G., Svergun, D. I., Mulder, F. A. A., Sussman, J. L. & Silman, I. (2008). Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. Biophysical Journal, 95(4), 1928-1944. https://doi.org/10.1529/biophysj.107.126995

Paquin, R., Ferrage, F., Mulder, F. A. A., Akke, M. & Bodenhausen, G. (2008). Multiple-timescale dynamics of side-chain carboxyl and carbonyl groups in proteins by ¹³C nuclear spin relaxation. Journal of the American Chemical Society, 130(47), 15805-15807. https://doi.org/10.1021/ja803794g

Lindman, S., Linse, S., Mulder, F. A. A. & André, I. (2007). pK_a Values for Side-Chain Carboxyl Groups of a PGB1 Variant Explain Salt and pH-Dependent Stability. Biophysical Journal, 92(1), 257-266. https://doi.org/10.1529/biophysj.106.088682

André, I., Linse, S. & Mulder, F. A. A. (2007). Residue-specific pK_a determination of lysine and arginine side chains by indirect ¹⁵N and ¹³C NMR spectroscopy: Application to apo calmodulin. Journal of the American Chemical Society, 129(51), 15805-15813. https://doi.org/10.1021/ja0721824

Helgstrand, M., Mandava, C. S., Mulder, F. A. A., Liljas, A., Sanyal, S. & Akke, M. (2007). The Ribosomal Stalk Binds to Translation Factors IF2, EF-Tu, EF-G and RF3 via a Conserved Region of the L12 C-terminal Domain. Journal of Molecular Biology, 365(2), 468-479. https://doi.org/10.1016/j.jmb.2006.10.025

Lindman, S., Linse, S., Mulder, F. A. A. & André, I. (2006). Electrostatic contributions to residue-specific protonation equilibria and proton binding capacitance for a small protein. Biochemistry, 45(47), 13993-14002. https://doi.org/10.1021/bi061555v

Brath, U., Akke, M., Yang, D., Kay, L. E. & Mulder, F. A. A. (2006). Functional dynamics of human FKBP12 revealed by methyl ¹³C rotating frame relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society, 128(17), 5718-5727. https://doi.org/10.1021/ja0570279

Lundström, P., Mulder, F. A. A. & Akke, M. (2005). Correlated dynamics of consecutive residues reveal transient and cooperative unfolding of secondary structure in proteins. Proceedings of the National Academy of Sciences, 102(47), 16984-16989. https://doi.org/10.1073/pnas.0504361102

Mulder, F. A. A., Bouakaz, L., Lundell, A., Venkataramana, M., Liljas, A., Akke, M. & Sanyal, S. (2004). Conformation and dynamics of ribosomal stalk protein L12 in solution and on the ribosome. Biochemistry, 43(20), 5930-5936. https://doi.org/10.1021/bi0495331

Mulder, F. A. A. & Akke, M. (2003). Carbonyl ¹³C transverse relaxation measurements to sample protein backbone dynamics. Magnetic Resonance in Chemistry, 41(10), 853-865. https://doi.org/10.1002/mrc.1252

Choy, W. Y., Mulder, F. A. A., Crowhurst, K. A., Muhandiram, D. R., Millett, I. S., Doniach, S., Forman-Kay, J. D. & Kay, L. E. (2002). Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques. Journal of Molecular Biology, 316(1), 101-112. https://doi.org/10.1006/jmbi.2001.5328

Mulder, F. A. A., Hon, B., Mittermaier, A., Dahlquist, F. W. & Kay, L. E. (2002). Slow internal dynamics in proteins: Application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society, 124(7), 1443-1451. https://doi.org/10.1021/ja0119806

Ayed, A., Mulder, F. A., Yi, G. S., Lu, Y., Kay, L. E. & Arrowsmith, C. H. (2001). Latent and active p53 are identical in conformation. Nature Structural and Molecular Biology, 8(9), 756-760. https://doi.org/10.1038/nsb0901-756

Mulder, F. A. A., Skrynnikov, N. R., Hon, B., Dahlquist, F. W. & Kay, L. E. (2001). Measurement of slow (μs-ms) 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. Journal of the American Chemical Society, 123(5), 967-975. https://doi.org/10.1021/ja003447g

Skrynnikov, N. R., Mulder, F. A. A., Hon, B., Dahlquist, F. W. & Kay, L. E. (2001). Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: Application to methionine residues in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society, 123(19), 4556-4566. https://doi.org/10.1021/ja004179p

Tollinger, M., Skrynnikov, N. R., Mulder, F. A., Forman-Kay, J. D. & Kay, L. E. (2001). Slow dynamics in folded and unfolded states of an SH3 domain. Journal of the American Chemical Society, 123(46), 11341-11352. https://doi.org/10.1021/ja011300z

Mulder, F. A., Mittermaier, A., Hon, B., Dahlquist, F. W. & Kay, L. E. (2001). Studying excited states of proteins by NMR spectroscopy. Nature Structural and Molecular Biology, 8(11), 932-935. https://doi.org/10.1038/nsb1101-932

Mulder, F. A., Ayed, A., Yang, D., Arrowsmith, C. H. & Kay, L. E. (2000). Assignment of 1H(N), 15N, 13C(alpha), 13CO and 13C(beta) resonances in a 67 kDa p53 dimer using 4D-TROSY NMR spectroscopy. Journal of Biomolecular N M R, 18(2), 173-176. https://doi.org/10.1023/A:1008317825976

van Tilborg, P. J., Czisch, M., Mulder, F. A. A., Folkers, G. E., Bonvin, A. M., Nair, M., Boelens, R. & Kaptein, R. (2000). Changes in dynamical behavior of the retinoid X receptor DNA-binding domain upon binding to a 14 base-pair DNA half site. Biochemistry, 39(30), 8747-8757. https://doi.org/10.1021/bi991550g

Mulder, F. A. A., Hon, B., Muhandiram, D. R., Dahlquist, F. W. & Kay, L. E. (2000). Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR. Biochemistry, 39(41), 12614-12622. https://doi.org/10.1021/bi001351t

Mulder, F. A. A., Schipper, D., Bott, R. & Boelens, R. (1999). Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins. Journal of Molecular Biology, 292(1), 111-123. https://doi.org/10.1006/jmbi.1999.3034

Mulder, F. A. A., van Tilborg, P. J., Kaptein, R. & Boelens, R. (1999). Microsecond time scale dynamics in the RXR DNA-binding domain from a combination of spin-echo and off-resonance rotating frame relaxation measurements. Journal of Biomolecular N M R, 13(3), 275-288. https://doi.org/10.1023/A:1008354232281

van Tilborg, P. J., Mulder, F. A. A., de Backer, M. M., Nair, M., van Heerde, E. C., Folkers, G., van der Saag, P. T., Karimi-Nejad, Y., Boelens, R. & Kaptein, R. (1999). Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation. Biochemistry, 38(7), 1951-1956. https://doi.org/10.1021/bi982526q

Brünger, A. T., Karimi-Nejad, Y., Mulder, F. A. A., Martin, J. R., Schipper, D. & Boelens, R. (1999). NMR Studies of the 269 Residue Serine Protease PB92 from Bacillus Alcalophilus. NMR in Supramolecular Chemistry, 526, 227-246. https://doi.org/10.1007/978-94-011-4615-9_14

Mulder, F. A. A., Graaf, R. A. D., Kaptein, R. & Boelens, R. (1998). An Off-resonance Rotating Frame Relaxation Experiment for the Investigation of Macromolecular Dynamics Using Adiabatic Rotations. Journal of Magnetic Resonance, 131(2), 351-357. https://doi.org/10.1006/jmre.1998.1380

Düx, P., Rubinstenn, G., Vuister, G. W., Boelens, R., Mulder, F. A. A., Hård, K., Hoff, W. D., Kroon, A. R., Crielaard, W., Hellingwerf, K. J. & Kaptein, R. (1998). Solution structure and backbone dynamics of the photoactive yellow protein. Biochemistry, 37(37), 12689-12699. https://doi.org/10.1021/bi9806652

Rubinstenn, G., Vuister, G. W., Mulder, F. A. A., Dux, P. E., Boelens, R., Hellingwerf, K. J. & Kaptein, R. (1998). Structural and dynamic changes of photoactive yellow protein during its photocycle in solution. Nature Structural Biology, 5(7), 568-570. https://doi.org/10.1038/823

Displaying results 51 to 100 out of 104

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Lise Refstrup Linnebjerg Pedersen