Laser-induced changes on the complex refractive indices of phase-change thin film

The refractive indices of crystalline phase-change films are usually obtained by thermal-induced crystallization. However, this is not accurate, because the crystallization of phase-change film in rewritable optical disks is laser induced. In this study, we use the initializer to crystallize the phase-change films. The dependence of the refractive index n and the extinction coefficient k of the phase-change films on the initialization conditions are studied. Remarkable changes of the refractive indices (especially k) are found when the initialization laser power density is 6.63 mW/mum(2) and the initialization velocity is 4.0 m/s. At the same time, the structure changes of the phase-change films are also studied. This dependence is explained by the structure change of the films. These results are significant in improving the accuracy of optical design and the thermal simulation of phase-change optical disks, as well as in the study of phase-change optical disks at shorter wavelengths. (C) 2003 Society of Photo-Optical Instrumentation Engineers.

Pivoting between Calmodulin Lobes Triggered by Calcium in the Kv7.2/Calmodulin Complex

Kv7.2 (KCNQ2) is the principal molecular component of the slow voltage gated M-channel, which strongly influences neuronal excitability. Calmodulin (CaM) binds to two intracellular C-terminal segments of Kv7.2 channels, helices A and B, and it is required for exit from the endoplasmic reticulum. However, the molecular mechanisms by which CaM controls channel trafficking are currently unknown. Here we used two complementary approaches to explore the molecular events underlying the association between CaM and Kv7.2 and their regulation by Ca2+. First, we performed a fluorometric assay using dansylated calmodulin (D-CaM) to characterize the interaction of its individual lobes to the Kv7.2 CaM binding site (Q2AB). Second, we explored the association of Q2AB with CaM by NMR spectroscopy, using N-15-labeled CaM as a reporter. The combined data highlight the interdependency of the N- and C-lobes of CaM in the interaction with Q2AB, suggesting that when CaM binds Ca2+ the binding interface pivots between the N-lobe whose interactions are dominated by helix B and the C-lobe where the predominant interaction is with helix A. In addition, Ca2+ makes CaM binding to Q2AB more difficult and, reciprocally, the channel weakens the association of CaM with Ca2+.