Research Highlights of Biological Physics Faculty

Single molecule force spectroscopy uses a microscopic AFM cantilever to grab individual proteins attached to a gold surface. This protein consists of eight repeats of the I27 domain of the heart muscle protein titin, a domain found in the extensible region of the striated muscle. The protein is stretched by retracting the cantilever from the sample surface at a constant velocity, and the force required to manipulate the molecule is monitored by the bending of the cantilever.

The mechanism of antimicrobial peptides was resolved by a combination of macroscopic and microscopic techniques: X-ray and neutron diffraction, oriented circular dichroism, and single GUV (giant unilamellar vesicle) experiment.  The new concept is that the elastic energy of lipid bilayer is a key to the mechanism.  We now widen the research to include membrane-active proteins and drugs.  We continue to explore novel X-ray/neutron techniques to resolve lipidic structures in membranes, such as membrane fusion intermediates, pores, and inhomogeneous lipid distribution, which are essential information for understanding membrane processes, such as fusion, apoptosis and drug effects.