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		Erwin London Professor B.A., Queens College of the City University of New York, 1974; Ph.D., Cornell University, 1980; Postdoctoral Fellow, Massachusetts Institute of Technology. Joint Appointment with Department of Biochemistry and Cell Biology. (631) 632-8564 Email: erwin.london@sunysb.edu Publications

	STRUCTURAL BIOLOGY MEMBRANE PROTEIN STRUCTURE, LIPID BILAYER STRUCTURE: Determining the Rules for Membrane Translocation and Membrane Protein Folding and Studies of Sphingolipid-Cholesterol Lipid Domains (Rafts) Our group is studying membrane protein structure and function by combining spectroscopic methods, such as fluorescence, with chemical, biochemical, immunochemical and molecular biological approaches. We are interested in determining membrane protein structure and the origin of specific lipid-protein and protein-protein interactions. At present, we are concentrating on protein toxins that penetrate and translocate across cell membranes, such as diphtheria toxin. Our aim is to understand the mechanism of membrane penetration by this toxin. This should have important implications for protein translocation in general, as well as the design of therapeutic agents and vaccines. One specific technique we are developing involves using antibody binding to study structure. Another involves the determination of the depth of groups by a fluorescence quenching technique These methods are being combined with site-directed mutagenesis in order to define the structure of the toxin in its membrane-inserted state. We are also using synthetic transmembrane helices. These studies are aimed at determining the basic rules for membrane protein folding. In a related project on the topic of membrane protein folding, we are systematically varying the sequence of synthetic transmembrane helices, and then comparing their conformation when incorporated into lipid bilayers using fluorescence spectroscopy and other methods. This project aims to reveal the basic principles behind membrane protein folding. In a third project we are studying membrane rafts. Rafts are sphingolipid and cholesterol rich domains that contain a special subset of membrane proteins. Rafts have critical roles in a variety of signal transduction and pathological processes, including viral and bacterial infection. We are studying the rules that govern the association of particular lipids and proteins in rafts, and developing methods to modify raft properties.

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