Aarhus University Seal

Daniel Erik Otzen

Professor, Ph.D.
Aarhus University
Interdisciplinary Nanoscience Centre
Department of Molecular Biology
Gustav Wieds Vej 10 C
8000 Aarhus C
Tel.: +45 2072 5238
Fax: +45 8612 3178


Daniel Erik Otzen (Denmark, 02-02-1969)

Private address : Minthøjvej 1, DK – 8210 Aarhus V, DENMARK. Tel. + 45 20725238.


1992    M.Sc. in Chemistry/Biotechnology, Aarhus University, Denmark

1995    PhD in Protein Science, Aarhus University and Cambridge University, UK

Professional details:

Professor of nanobiotechnology, iNANO; Department of Molecular Biology, Aarhus University, Gustav Wieds Vej 14, 8000 Aarhus C. Email: dao@inano.au.dk; web: http://www.proteins.dk

Professional experience:

1995-1997                   Research Chemist, Novo Nordisk A/S

1997-2000                   Post-doctoral fellow at Lund University

2000-2004                   Associate Professor, Department of Life Sciences, Aalborg University.

2004-2007                   Professor, Department of Life Sciences, Aalborg University

2007-                           Professor, iNANO, Aarhus University.

2006-2011 and 2013- Adjunct Professor, Copenhagen University

2007-2012                   Adjunct Professor, Aalborg University

Areas of expertise:

Pathological and functional fibrillation and aggregation of proteins.

Protein stability and formulation.

Protein-surfactant and protein-lipid interactions.

Biophysics of membrane proteins, including stability and mechanism of insertion, folding and association in lipid bilayers and detergent micelles.

Fellowships and awards:

2014    Eliteforskerpris (Elite Researcher Prize), Danish Ministry of Science and Innovation

2010    Member, Royal Danish Society of Science and Letters

2009    The Research Prize of the Alzheimer Research Foundation

2006    Carlsberg Biotechnology Prize

2003    Silver Medal, Royal Danish Society of Sciences and Letters.

2003    EMBO Young Investigator


2009-               Leader, Lundbeck network for Bacterial Amyloid

2006-2011       Consortium Leader, Innovation Consortium CureND

2002-2007       Director of Doctoral School of Biotechnology, Aalborg University.

2013-               Coordinator, Marie Curie ITN project TOPIC (2 European Industrial Doctorates)

Scholarly activity:

Reviewer for >50 different journals. Editor of Biochimica et Biophysica Acta and Biophysical Chemistry. Since 2013 member of Danish Research Council (FNU – Natural Sciences).

Publication record:

1 edited book, 10 book chapters and > 245 articles in international peer-reviewed journals since 1993. These include: 1 in Nature Communications, 3 in JACS, 2 in Angew. Chemie, 10 in PNAS, 2 in Molecular Microbiology, 15 in J. Biol. Chem., 22 in J. Mol. Biol., 19 in Biochemistry and 13 reviews. >6000 citations, H-factor 49 (Google Scholar).

Research group and facilities:

Heads research group with 3 post-docs, 10 PhD students, 2 M.Sc. students and 1 lab technician. Has supervised 27 PhD students and > 40 M.Sc. students. Research equipment includes optical spectroscopy, mechano-acoustic instrumentation, calorimetry and imaging equipment in combination with rapid reaction apparatus. This is combined with protein engineering and detailed mechanistic interpretation of the data.

Daniel Otzen’s 10 most important publications 2013-2016:

  1. Schafer, N., Truong, H., Otzen, D.E., Lindorff-Larsen, K. and Wolynes, P. (2016) Topological constraints and modular structure in the folding and functional motions of GlpG, an intramembrane protease, Natl. Acad. Sci. USA 113, in press.
  2. Paslawski, W., Kristensen, J.V., Lillelund, O., Schafer, N., Baker, R., Urban, S., Otzen, D.E. (2015) Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and non-native loops, Natl. Acad. Sci. USA,112, 7978-83.
  3. Tian, , P., Boomsma, W., Wang, Y., Otzen, D. E., Jensen, M. H., and Lindorff-Larsen, K. (2015) Structure of a Functional Amyloid Protein Subunit Computed Using Sequence Variation, Am. Chem. Soc. 137, 22-25.
  4. Paslawski, W., Mysling, S., Thomsen, K., Jørgensen, T. J. D., and Otzen, D. E. (2014) Co-existence of two different α-synuclein oligomers with different core structures determined by Hydrogen/Deuterium Exchange Mass Spectrometry, Angew Chem Int Ed Engl 53, 7560-7563.
  5. Paslawski, W., Andreasen, M., Nielsen, S. B., Lorenzen, N., Thomsen, K., Kaspersen, J. D., Pedersen, J. S., and Otzen, D. E.(2014) High stability and cooperative unfolding of cytotoxic α-synuclein oligomers Biochemistry 53, 6252-6263.
  6. Lorenzen, N., Nielsen, S. B., Yoshimura, Y., Andersen, C. B., Betzer, C., Vad, B. S., Kaspersen, J. D., Christiansen, G., Pedersen, J. S., Jensen, P. H., Mulder, F. A., and Otzen, D. E. (2014) How epigallogatechin gallate can inhibit α-synuclein oligomer toxicity in vitroBiol. Chem. 289, 21299-21310.
  7. Lorenzen, N., Nielsen, S. B., Buell, A. K., Kaspersen, J. D., Arosio, P., Vad, B. S., Paslawski, W., Christiansen, G., Valnickova-Hansen, Z., Andreasen, M., Enghild, J. J., Pedersen, J. S., Dobson, C. M., Knowles, T. J., and Otzen, D. E. (2014) The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation, Am. Chem. Soc. 136, 3859-3868.
  8. , Sarr, M., Jörnvall, H., Wennmalm, S., Widengren, J., Meng, Q., Rising, A., Otzen, D., Knight, S. D., Jaudzems, K., and Johansson, J. (2014) Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation, Nature Comm. 5, 3254.
  9. Kaspersen, J. D., Pedersen, J. N., Hansted, J. G., Nielsen, S. B., Sakthivel, S., Wilhelm, K., Knyazeva, E. L., Permyakov, E. A., Permyakov, E. A., Oliveira, C. L. P., Morozova-Roche, L., Otzen, D. E., and Pedersen, J. S. (2014) Generic structures of liprotides, complexes between partially denatured proteins and oleic acid: a fatty acid core with a shell of disordered proteins, ChemBioChem 18, 2693-2702.
  10. Zhang, S., Andreasen, M., Nielsen, J. T., Liu, L., Nielsen, E. H., Song, J., Ji, G., Sun, F., Skrydstrup, T., Besenbacher, F., Nielsen, N. C., Otzen, D. E., and Dong, M. (2013) Coexistence of ribbon and helical fibrils originating from hIAPP(20-29) revealed by quantitative nanomechanical atomic force microscopy, Proc Natl Acad Sci U S A 110, 2798-2803.