Thursday, March 16, 2006, 1:30 pm — Small Seminar Room, Bldg. 510
Lipid bilayer is the structural matrix of cell membranes. The structure is flexible, robust, and stable against puncture. Yet there are gene-coded proteins, called antimicrobial peptides, whose function appears to be punching holes in lipid bilayers. Based on X-ray, neutron and optical studies, we have deduced the structural basis of this function. Peptides at first bind to the bilayer’s interface without making pores. Only when the concentration reaches a threshold, pores begin to form. I will discuss the experiments for the structural basis of the mechanism, and the thermodynamics for this cooperative (micellar-like) phenomenon. Our on-going experiment at X21 is trying to resolve the pore structures.
Hosted by: Masafumi Fukuto
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