We utilize femtosecond time-resolved coherent anti-Stokes Raman spectroscopy (CARS) to study the vibrational dynamics of methanol-water solutions. We measure the beat wavenumbers between Raman modes and coherence decay rates of C-H stretch modes (at 2835 cm −1 and 2943 cm −1 ) in methanol. We observe a qualitative dependence of the coherence relaxation rate on the concentration of methanol in its water solution. This may be linked to the formation of the recently observed supramolecular structures in methanol-water mixtures.

Biosensors based on the principle of surface plasmon resonance (SPR) detection were used to measure biomolecular interactions in sarcomeres and changes of the dielectric constant of tubulin samples with varying concentration. At SPR, photons of laser light efficiently excite surface plasmons propagating along a metal (gold) film. This resonance manifests itself as a sharp minimum in the reflection of the incident laser light and occurs at a characteristic angle.The dependence of the SPR angle on the dielectric permittivity of the sample medium adjacent to the gold film allows the monitoring of molecular interactions at the surface. We present results of measurements of cross-bridge attachment/detachment within intact mouse heart muscle sarcomeres and measurements on bovine tubulin molecules pertinent to cytoskeletal signal transduction models.

We have developed a surface plasmon resonance (SPR) system to monitor the cross-bridge attachment/detachment process within intact sarcomeres from mouse heart muscle. SPR occurs when laser light energy is transferred to surface plasmons that are resonantly excited in a metal (gold) film. This resonance manifests itself as a minimum in the reflection of the incident laser light and occurs at a characteristic angle. The angle of the SPR occurrence depends on the dielectric permittivity of the sample medium adjacent to the gold film. Purified sarcomeric preparations are immobilized onto the gold film in the presence of a relaxing solution. Replacement of the relaxing solution with increasing Ca(2+) concentration solution activates the cross-bridge interaction and produces an increase in the SPR angle. These results imply that the interaction of myosin heads with actin within an intact sarcomere changes the dielectric permittivity of the sarcomeric structure. In addition, we further verify that SPR measurements can detect the changes in the population of the attached cross-bridges with altered concentrations of phosphate, 2,3-butanedione monoxime, or adenosine triphosphate at a fixed calcium concentration, which have been shown to reduce the force and increase the cross-bridge population in attached state. Thus, our data provide the first evidence that the SPR technique allows the monitoring of the cross-bridge attachment/detachment process within intact sarcomeres.

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