This page is printed on Sep 26, 2017 from http://www.bionmr.chem.au.dk/bionmr/group/krestenb/index.php

 
 

 
Name:
Profession:Ph.d. Student
Email:krestenb@chem.au.dk
Homepage:None
Work address: Laboratory for Biomolecular NMR Spectroscopy
Department of Chemistry
University of Aarhus
Langelandsgade 140, DK-8000 Aarhus C, Denmark
Home address: Høegh Guldbergsgade 49 2. 2
8000 Aarhus C
+4522339992
Office: 1512-222
Office phone: +4589423872
Dept. duties:

Research

NMR spectroscopy of insoluble membrane structures
 

Curriculum Vitae


Personal data

Name:Kresten Bertelsen
Nationality:Danish
Date of Birth:25th April 1981
Marital status:Not married


Education

2005:Bachelor in nanoscience
:


Appointments

:

Publications

Publications in Reviewed Journals

  1. K. Bertelsen, J. Dorosz, S. K. Hansen, N. C. Nielsen, and T. Vosegaard, PLOS ONE 7, e47745 (2012).
    Mechanisms of Peptide-Induced Pore Formation in Lipid Bilayers Investigated by Oriented 31P Solid-State NMR Spectroscopy
  2. K. Bertelsen, B. Vad, E. H. Nielsen, S. K. Hansen, T. Skrydstrup, D. E. Otzen, T. Vosegaard, and N. C. Nielsen, J. Phys. Chem. B 115, 1767-1774 (2011).
    Long-Term-Stable Ether-Lipid vs Conventional Ester- Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides
  3. B. S. Vad, K. Bertelsen, C. H. Johansen, J. M. Pedersen, T. Skrydstrup, N. C. Nielsen, and D. E. Otzen, Biophysical Journal 98, 576 (2010).
    Pardaxin Permeabilizes Vesicles More Efficiently by Pore Formation than by Disruption
  4. B. Vad, K. Bertelsen, C.H. Johansen, J.M. Pedersen, T. Skrydstrup, N.C. Nielsen, and D.E. Otzen, Biophysical Journal 98, 576-585 (2010).
    The Antimicrobial Peptide Pardaxin Displays a pH- and Lipid-Dependent Interaction with Lipid Bilayers
  5. B. S. Vad, L. A. Thomsen, K. Bertelsen, M. Franzmann, J. M. Pedersen, S. B. Nielsen, T. Vosegaard, Z. Valnickova, T. Skrydstrup, J. J. Enghild, R. Wimmer, N. C. Nielsen, and D. E. Otzen, Biochim. Biophys. Acta 1804, 806-820 (2010).
    Divorcing Folding from Function: How Acylation Affects the Membrane-perturbing Properties of an Anti-microbial Peptide
  6. B. Vad, K. Bertelsen, C.H. Johansen, J.M. Pedersen, T.S. Skrydstrup, N.C. Nielsen, and D.E. Otzen, Biophysical Journal 98, 576-585 (2009).
    Pardaxin permeabilizes vesicles more efficiently by pore formation than by disruption
  7. J. Dittmer, L. Thøgersen, J. Underhaug, K. Bertelsen, T. Vosegaard, J. M. Pedersen, B. Schiøtt, E. Tajkhorshid, T. Skrydstrup, and N. C. Nielsen, J. Phys. Chem. B 113, 6928-2937 (2009).
    Incorporation of Antimicrobial Peptides into Membranes: A Combined Liquid-State NMR and Molecular Dynamics Study of Alamethicin in DMPC/DHPC Bicelles
  8. K. Bertelsen, J. M. Pedersen, B. S. Rasmussen, T. Skrydstrup, N. C. Nielsen, and T. Vosegaard, J. Am. Chem. Soc. 129, 14717-14723 (2007).
    Membrane-Bound Conformation of Peptaibols with Methyl-Deuterated a-Amino Isobutyric Acids by 2H MAS Solid-State NMR Spectroscopy
  9. K. Bertelsen, J. M. Pedersen, N. C. Nielsen, and T. Vosegaard, J. Magn. Reson. 184, 273-279 (2007).
    2D separated-local field spectra from projections of 1D experiments