Heinrich Roder
Department of Molecular Therapeutics
Fox Chase Cancer Center
United States of America
Biography
Heinrich Roder,Educational Background PhD, Biophysics, Swiss Federal Institute of Technology (ETH), Zürich, Switzerland, 1981 Memberships :Biophysical Society. American Association for the Advancement of Science. Protein Folding Consortium. Protein Society. American Chemical Society. Honors & Awards: Site Visit, NIH Bioengineering Science and Technology IRG, 2015. NSF Chemistry of Life Processes Panel, 2014. Keynote Speaker, NJACS, Princeton NJ, 2014. External Review Committee, Department of Biochemistry, University of Zurich, Switzerland, 2013. NIH NHLBI Board of Counselors, 2008.
Research Interest
Protein folding, structure and function. Mechanisms of protein folding, focusing on fast kinetics and early structural events. Protein structure, dynamics and ligand interactions, focusing on signaling adapters. Functional roles of intrinsically disordered protein regions. Methods used include NMR spectroscopy, H/D exchange, fluorescence and rapid mixing.
Publications
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Montalvo, G. L., Gai, F., Roder, H., & DeGrado, W. F. (2013). Slow Folding–Unfolding Kinetics of an Octameric β-Peptide Bundle. ACS chemical biology, 9(1), 276-281.
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Fazelinia, H., Xu, M., Cheng, H., & Roder, H. (2013). Ultrafast hydrogen exchange reveals specific structural events during the initial stages of folding of cytochrome c. Journal of the American Chemical Society, 136(2), 733-740.
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Honda, R. P., Xu, M., Yamaguchi, K. I., Roder, H., & Kuwata, K. (2015). A native-like intermediate serves as a branching point between the folding and aggregation pathways of the mouse prion protein. Structure, 23(9), 1735-1742.
