- Senior Investigator, Laboratory of Membrane Biochemistry and Biophysics
Dr. Gawrisch was born in Freyburg, Germany in 1950. He received training in biophysics in the laboratory of Lev A. Blumenfeld and a Master's Degree in Physics from Moscow State University, Russia, in 1975. In Leipzig, at the laboratories of Gotthard Klose and Klaus Arnold he was trained in membrane biophysics and Nuclear Magnetic Resonance (NMR) and received a Ph.D. in Physics in 1979 and the Habilitation in Physics in 1986 both from the University of Leipzig, Germany. Until 1989 he served as Docent in Physics and Biophysics at the University of Leipzig. In 1989 he joined the laboratory of Adrian Parsegian at the Division of Computer Research and Technology and later the NMR laboratory of James Ferretti at the National Heart Lung and Blood Institute of the National Institutes of Health in Bethesda, Maryland. From 1993-1998 he was a Tenure Track Investigator heading the Section of NMR of the Laboratory of Membrane Biochemistry and Biophysics at the National Institute on Alcohol Abuse and Alcoholism of NIH. He is currently the Chief of the Laboratory of Membrane Biochemistry and Biophysics and the Chief of the Section of NMR in the laboratory. For his achievements in lipid biophysics he received the 2007 Avanti Award in Lipids of the Biophysical Society.
Academic Articles114
- (2012). The role of the lipid matrix for structure and function of the GPCR rhodopsin. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES. 1818(2), 234-240.
- (2011). Structure and Dynamics of Cholesterol-Containing Polyunsaturated Lipid Membranes Studied by Neutron Diffraction and NMR. JOURNAL OF MEMBRANE BIOLOGY. 239(1-2), 63-71.
- (2010). A Lipid Pathway for Ligand Binding Is Necessary for a Cannabinoid G Protein-coupled Receptor. JOURNAL OF BIOLOGICAL CHEMISTRY. 285(23), 17954-17964.
- (2010). Contribution of Membrane Elastic Energy to Rhodopsin Function. BIOPHYSICAL JOURNAL. 99(3), 817-824.
- (2010). Preparation of stable isotope-labeled peripheral cannabinoid receptor CB2 by bacterial fermentation. PROTEIN EXPRESSION AND PURIFICATION. 70(2), 236-247.