The Jackson Laboratory: Alex Watson

Magnus Kjaergaard

Magnus Kjaergaard

Postdoctoral Research Assistant (shared with the Klenerman lab)
M.Sci. & Ph.D., University of Copenhagen, Denmark
Room B52 • +44 (0)1223 336421 •

Present Research

  1. Studying the effects of molecular chaperones on amyloid oligomers using single-molecule fluorescence spectroscopy


  • Kjaergaard, M., Poulsen, F.M. and Kragelund, B.B. (2011)
    "Temperature induced transitions in disordered proteins probed by NMR spectroscopy"
    Methods in Molecular Biology, (in press)
  • Kjaergaard, M., Poulsen, F.M. and Kragelund, B.B. (2011)
    "Temperature induced transitions in disordered proteins probed by NMR spectroscopy and secondary chemical shift analyses"
    Methods in Molecular Biology, (in press)
  • Kjaergaard, M. & Poulsen, F.M. (2011)
    "Disordered proteins studied by chemical shifts"
    Prog. NMR Spec., [Epub ahead of print]
  • Gardsvoll, H., Kjaergaard, M., Jacobsen, B., Kriegbaum, M.C., Huang, M. & Ploug, M. (2011)
    "Mimicry of the regulatory role of urokinase in lamellipodia formation by introduction of a non-native interdomain disulfide bond in its receptor"
    J. Biol. Chem., [Epub ahead of print]
  • Kjaergaard, M., Iesmantavicius, V., and Poulsen, F.M. (2011)
    "The interplay between transient a-helix formation and side chain rotamer distributions in disordered proteins probed by methyl chemical shifts"
    Protein Science, Protein Science, Sep 6. doi: 10.1002/pro.726
  • Kjaergaard, M. & Poulsen, F.M.(2011)
    "Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution"
    J. Biomol. NMR. 50(2):157-65.
  • Norholm, A.B., Hendus-Altenburger, R., Bjerre, G., Kjaergaard, M.,Pedersen, S.F. and Kragelund, B.B. (2011)
    "The intracellular distal tail of the Na+/H+ exchanger NHE1 is intrinsically disordered: implications for NHE1 trafficking"
    Biochemistry 50(17):3469-80.
  • Kjaergaard, M., Brander,S. and Poulsen, F.M. (2011)
    "Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH"
    J. Biomol. NMR 49(2):139-149.
  • Cervantes C.F., Bergqvist, S., Kjaergaard, M., Kroon, G., Sue, S.C., Dyson, H.J. and Komives, E.A. (2011)
    "The RelA nuclear localization signal folds upon binding to IkBa"
    J. Mol. Biol. Jan 21;405(3):754-64.
  • Kjaergaard, M., Nørholm, A.B., Hendus-Altenburger, R., Pedersen, S.F., Poulsen, F.M. and Kragelund, B.B. (2010)
    "Temperature dependent structural changes in intrinsically disordered proteins: Formation of a-helices or loss of polyproline II?"
    Protein Science. Aug;19(8):1555-64.
  • Kjaergaard, M., Teilum, K. and Poulsen, F.M. (2010)
    "Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP"
    Proc Natl Acad Sci USA. Jul 13;107(28):12535-40
  • Truhlar, S.M., Cervantes, C.F., Torpey, J.W., Kjaergaard, M. and Komives, E.A. (2008)
    "Rapid mass spectrometric analysis of 15N-Leu incorporation fidelity during preparation of specifically labeled NMR samples"
    Protein Science. 17(9):1636-9
  • Kjaergaard, M., Hansen, L.V., Jacobsen, B., Gårdsvoll, H., Ploug, M. (2008)
    "Structure and ligand interactions of the urokinase receptor;
    Frontiers in Bioscience. 5441-5461, May 1.
  • Jacobsen, B., Kjaergaard, M., Gårdsvoll, H. and Ploug,M. (2008)
    "Structure and inhibition of the urokinase-type plasminogen activator receptor (uPAR)"
    The Cancer Degradome-Proteases and Cancer Biology , D. Edwards, G. Høyer-Hansen, F. Blasi and B.F. Sloane (eds), Springer Verlag
  • Kjaergaard, M., Gårdsvoll, H., Hirschberg, D., Nielbo, S., Mayasundari, A., Peterson, C.B., Jansson, A., Jørgensen, T.J.D., Poulsen, F.M., Ploug, M. (2007)
    "Solution structure of recombinant Somatomedin B domain from vitronectin produced in Pichia pastoris"
    Protein Science. 16(9) 1934-45
  • Bergqvist, S., Croy, C.H., Kjaergaard, M., Huxford, T., Ghosh, G., Komives, E.A. (2006)
    "Thermodynamics reveal that helix four in the NLS of NF-kappaB p65 anchors IkappaBalpha, forming a very stable complex"
    J. Mol. Biol. Jul 7;360(2):421-34.