Prof. Dr. Henrike Heise

Institute of Physical Biology
Heinrich Heine University Düsseldorf
Universitätsstr. 1
40225 Düsseldorf

phone: +49(0)211-81-10810
fax: +49(0)211-81-15167
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Institute of Neurosciences and Biophysics (INB)/ Institute 2: Molecular Biophysics (INB-2)
Research Center Jülich GmbH
52425 Jülich

+49(0)2461-61-4658
+49(0)2461-61-2023


 website


Curriculum Vitae & Publications

 publication list

Expertise in Structural Biology

  • Solid-State NMR Spectroscopy

Main areas of research interest

  • Solid-State NMR Spectroscopy technique development
  • Study of amyloid proteins
  • Structure, dynamics and topology of membrane proteins

Research Group and Equipment

 For detailed information click here...

BioStruct Research Project

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Important references

  • Heise, H., Hoyer, W., Becker, S., Andronesi, O., Riedel, D. & Baldus, M. (2005). Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR. Proc. Natl. Acad. Sci. U.S.A. 102, 15871-15876.
  • Heise, H., Seidel, K., Etzkorn, M., Becker, S. & Baldus, M. (2005). 3D NMR spectroscopy for resonance assignment and structure elucidation of proteins under MAS: novel pulse schemes and sensitivity considerations. J. Magn. Reson. 173, 64-74.
  • Andronesi, O. C., Becker, S., Seidel, K., Heise, H., Young, H. S. & Baldus, M. (2005). Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy. J. Am. Chem. Soc. 127, 12965-12974.
  • Heise, H. (2008). Solid-state NMR spectroscopy of amyloid proteins. ChemBioChem 9, 179-189.
  • Heise, H., Celej, M. S., Becker, S., Riedel, D., Pelah, A., Kumar, A., Jovin, T. M. & Baldus, M. (2008). Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant α-synuclein. J. Mol. Biol. 380, 444-450.

Foto: Hanne Horn

Last updated: 28.09.2012, 10:37
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