Carnegie Mellon University

Mathias  Loesche

Dr. Mathias Loesche

Professor, Physics and Biomedical Engineering

Address
Wean Hall 6311
Carnegie Mellon University
5000 Forbes Avenue
Pittsburgh, PA 15213

Education

  • M.S., Undergraduate School in Physics (Ulm Univ., Germany), 1983
  • Ph.D., Graduate Program, Biophysics (TU Munich, Germany), 1986
  • Postdoctoral Researcher, Biophysics (UC San Diego, CA), 1986-1988
  • Asst. Professor, Phys. Chem. (Univ. Mainz, Germany), Habilitation, 1994
  • Professorship (tenure), Exp. Physics (Leipzig University, Germany), 1995

Bio

Mathias Lösche obtained his Ph.D. in Physics at the Technical University in Munich (Germany) and, after a post-doctoral appointment in Biophysics at UCSD, joined the Chemistry Department of Mainz University (Germany), where he developed methods of surface-sensitive x-ray and neutron scattering for molecular-scale studies of soft matter interface layers. After obtaining his Habilitation in Mainz, he took up a tenured professorship in Physics at Leipzig University, where he led the Biomembrane Physics Group.

In 2002, on leave from Leipzig University, he served as the Director of the NIH-funded CNBT Research Consortium at the NIST Center for Neutron Research (Gaithersburg, MD). He joined the Physics Dept. of CMU in 2005, remains connected with the NCNR as a NIST Associate and is a faculty member of the MB+SB (Molecular Biophysics and Structural Biology) Graduate Program jointly operated by the University of Pittsburgh and Carnegie Mellon.

Research

The Lösche Lab – also known as Supramolecular Structures Laboratory – is broadly interested in the structural biology of membrane-related cellular processes. The group has a presence at two locations, the CMU Physics Dept. and the NIST Center for Neutron Research (NCNR). We have engineered substrate-supported lipid bilayer systems that resemble planar biomembranes, which we study for their structure, dynamics and functionality. Our hallmark technology is neutron reflection, performed at national facilities such as the NCNR, which enables us to characterize protein complexes in their natural, fluid membrane environment. In combination with computer modeling and simulation, this technique enables us to characterize such systems with atomistic models. We collaborate with biomedical collaborators across the nation and internationally.

Research Interests: biomaterials; bionanotechnology; structural biology; membrane protein complexes

  

Awards and Recognition

  • NIST Associate

  • APS Fellow