We have developed computer animation techniques to analyze the long-range electron transfer in proteins. In this work, electron tunneling in proteins was simulated by the Feynman path integral method with the Metropolis Monte Carlo technique. This simulation method was proposed by Kuki and Wolynes (1987). We applied this method to Ru-modified cytochrome c under artificial potentials in the protein, and introduced trimmed parametric surfaces to describe electron transfer pathways obtained by the above simulation. In order to observe the pathways in detail, a computer animation was produced in which a camera eye is moving along one of the electron paths in the protein.
αB-Crystallin (CryAB) is a major stress protein in cardiac myocytes. Under pathological stress such as ischemia, it acts as a molecular chaperone to suppress protein aggregation at the Z-line and at the I-band region of myofibril and at the intercalated disk. We report here that CryAB-like immunoreactivity also exists as a relatively weak but distinct signal at the M-line in isolated Syrian hamster ventricular myocytes, using a new laser confocal immunofluorescence microscope with high resolution. Our electron microscopic examination revealed that mitochondria in the isolated myocytes carried evidence of mild ischemia. Immunoblot analysis using a polyclonal antibody against CryAB detected a single protein with molecular mass of 21kDa in Syrian hamster left ventricle. The novel localization of CryAB-like immunoreactivity in the cardiac myofibril and its possible relation to ischemia may shed light on a yet to be unraveled chaperonic function of this stress protein in the heart.