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Name:Jakob Toudahl Nielsen
Profession:Post doc
Work address: Laboratory for Biomolecular NMR Spectroscopy
Department of Chemistry
University of Aarhus
Langelandsgade 140, DK-8000 Aarhus C, Denmark
Home address:
Office: 512-215
Office phone: 89425528
Dept. duties:



Curriculum Vitae

Personal data

Name:Jakob Toudahl Nielsen
Date of Birth:211075
Marital status:Married


2001-2006:Ph.D., Syddansk Universitet




Publications in Reviewed Journals

  1. N. Kalashnyk, J.T. Nielsen, E.H. Nielsen, T. Skrydstrup, D.E. Otzen, E. Lægsgaard, C. Wang, F. Besenbacher, N.C. Nielsen, and T. Linderoth, ACS Nano 6, 6882-6889 (2012).
    Scanning Tunneling Microscopy Reveals Single-Molecule Insights into the Self-Assembly of Amyloid Fibrils
  2. M. Andreasen, S. Nielsen, T. Mittag, M. Bjerring, J.T. Nielsen, S. Zhang, E.H. Nielsen, M. Jeppesen, G. Christiansen, M. Dong, N.C. Nielsen, T. Skrydstrup, and D. Otzen, Biophys. Biochem. Acta 1824, 274-285 (2012).
    Modulation of Fibrillation of hIAPP Core Fragments by Chemical Modification of the Peptide Backbone
  3. J.T. Nielsen, H.R. Eghbalnia, and N.C. Nielsen, Progr. NMR Spectrosc. 60, 1-28 (2012).
    Chemical shift prediction method for protein structure calculation and quality assessment using an optimally parametrized force field.
  4. L. Jiang, A.S.P. Svane, H.P. Sørensen, J.K. Jensen, M. Hosseini, Z. Chen, C. Weydert, J.T. Nielsen, A. Christensen, C. Yuana, K.J. Jensen, N.C. Nielsen, A. Malmendal, M. Huang, and P.A. Andreasen, J. Mol. Biol. 412, 335-350 (2011).
    The Binding Mechanism of a Peptidylic Cyclic Serine Protease Inhibitor
  5. C. Kehlet, J. T. Nielsen, Z. Tosner, and N. C. Nielsen, J. Phys. Chem. Lett 2, 543-547 (2011).
    Resolution-Enhanced Solid-State NMR 13C-13C Correlation Spectroscopy by Optimal Control Dipolar-Driven Spin-State-Selective Coherence Transfer
  6. J. T. Nielsen, M. Bjerring, M. D. Jeppesen, R. O. Pedersen, J. M. Pedersen, K. L. Hein, T. Vosegaard, T. Skrydstrup, D. E. Otzen, and N. C. Nielsen, Angew. Chem. Intl. Ed. 48, 2118-2121 (2009).
    Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy