Professor of Physics and Biomedical Engineering (courtesy)
Associate, National Institute of Standards and Technology
Biological Physics Experiment
Supramolecular Structures Laboratory
6311 Wean Hall
assistant: Amanda Bodnar, 412-268-8367
Education & Professional Experience
PhD: Technical University of Munich (Germany), Biophysics (1986)
Habilitation: Mainz University (Germany), Physical Chemistry (1994)
Member, American Physical Society (APS); Biophysical Society (U.S.); American Chemical Society (ACS); Neutron Scattering Society of America (NSSA); German Physical Society (DPG); German Biophysical Society (DGfB)
Fellow, American Physical Society
Professor of Biomedical Engineering, Carnegie Mellon University, 2008–
Professor of Physics, Carnegie Mellon University, 2005–
Director, CNBT Consortium, The NIST Center for Neutron Research, 2002–06
Research Professor (Biophysics), Johns Hopkins University, 2002–05
Associate Professor (Experimental Physics), Leipzig University, 1994–2005
Assistant Professor (Physical Chemistry), Mainz University, 1988–94
Post-doctoral Research (Biophysics): UC San Diego, 1986–88
In the past few decades, biology has revolutionalized our understanding of how living matter organizes itself to achieve the most astounding feat on the planet: Create intricate, organized structures that self-replicate and continuously develop further – despite the dictum of entropy which inequitably favors disorder over order. Are living systems therefore somehow miraculously exempt from the laws of Physics? – Not at all! Rather, they have "learned" to exploit loopholes in the dictate of entropy in truly stunning ways! Biological Physics is a fascinating branch of "mainstream Physics" that tries to solve the underlying puzzles.
M. Barros, F. Heinrich, S. A. K. Datta, A. Rein, I. Karageorgos, H. Nanda, and M. Lösche, Membrane binding of HIV-1 matrix protein: Dependence on bilayer composition and protein lipidation, J. Virol. 90 (2016), 4544 - 4555.
Y. Shen, et al., PlyC, a bacteriophage endolysin that is internalized by epithelial cells and retains bacteriolytic activity against intracellular streptococci, eLife 5 (2016), e13152.
R. A. Dick, M. Barros, D. Jin, M. Lösche, and V. M. Vogt, Membrane binding of the Rous sarcoma virus Gag protein is cooperative and dependent on the SPA domain, J. Virol. 90 (2016), 2473 - 2485.
F. Heinrich, S. Chakravarthy, H. Nanda, A. Papa, P. P. Pandolfi, A. H. Ross, R. K. Harishchandra, A. Gericke, and M. Lösche, The PTEN tumor suppressor forms homodimers in solution, Structure 23 (2015), 1952 - 1957.
H. Nanda, F. Heinrich, and M. Lösche, Membrane association of the PTEN tumor suppressor: Neutron scattering and MD simulations reveal the structure of protein-membrane complexes, Methods 77–78 (2015), 136 - 146.
F. Heinrich, H. Nanda, H. Z. Goh, C. Bachert, M. Lösche, and A. D. Linstedt, Myristoylation restricts orientation of the GRASP domain on membranes and promotes membrane tethering, J. Biol. Chem. 289 (2014), 9683 - 9691.
A. Kalinowski, Z. Qin, K. Coffey, R. Kodali, M. J. Buehler, M. Lösche, K. N. Dahl, Calcium causes a conformational change in lamin A tail domain that promotes farnesyl-mediated membrane association, Biophys. J. 104 (2013), 2246 - 2253.
S. S. Shenoy, H. Nanda and M. Lösche, Membrane association of the PTEN tumor suppressor: Electrostatic interaction with phosphatidylserine-containing bilayers and regulatory role of the C-terminal tail, J. Struct. Biol. 180 (2012), 394 - 408.
S. S. Shenoy, P. Shekhar, F. Heinrich, M.-C. Daou, A. Gericke, A. H. Ross, and M. Lösche, Membrane association of the PTEN tumor suppressor: Molecular details of the protein-membrane complex from SPR binding studies and neutron reflection, PLoS One 7 (2012), e32591.
P. N. Yaron, B. D. Holt, P. A. Short, M. Lösche, M. F. Islam, and K. N. Dahl, Single wall carbon nanotubes enter cells by endocytosis and not membrane penetration, J. Nanobiotechn. 9 (2011), 45-1 - 15.