Prof. Dr. Henrike Heise
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Institute of Physical Biology Heinrich Heine University Düsseldorf Universitätsstr. 1 40225 Düsseldorf +49(0)211-81-10810 +49(0)211-81-15167![]() 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
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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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