Browsing by Author "Tu, Jing-Ru"
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Item type:Item, Crystal Growth of Lysozyme Controlled by Laser Trapping(2014-01-01) ;Tu, Jing-Ru ;Miura, Atsushi ;Yuyama, Ken-ichi ;Masuhara, HiroshiSugiyama, TerukiWe demonstrate the growth of a tetragonal crystal of hen egg-white lysozyme (HEWL) in D2O buffer solution controlled by laser trapping with a focused continuous-wave (CW) near-infrared (NIR) laser beam. The focal spot was located at 10 mu m away from the edge of the target crystal that was generated spontaneously, and the crystal growth was observed although the focal spot size was much smaller than the distance. The growth rate of (101) and {110} faces of the tetragonal crystal was examined with various laser powers and polarizations. The rate observed under the irradiation was much different from those in spontaneous growth, namely, the growth rate of the {1 10} face showed a large decrease or increase depending on the irradiation time. The dynamics and mechanism of this unusual crystal growth behavior is discussed from the viewpoint of a large stable domain formation of the HEWL liquidlike clusters through liquid nucleation and growth and by considering the anisotropy of the cluster domain.Item type:Item, Dynamics and Mechanism of Laser Trapping-Induced Crystal Growth of Hen Egg White Lysozyme(2015-10-01) ;Tu, Jing-Ru ;Yuyama, Ken-ichi ;Masuhara, Hiroshi ;Sugiyama, Teruki應用化學系We propose the dynamics and mechanism of laser trapping-induced crystal growth of hen egg-white lysozyme (HEWL). A continuous-wave near-infrared laser beam is used as a trapping light source and focused at a point 10 mu m away from a target tetragonal HEWL crystal that is spontaneously generated in solution. Laser trapping of HEWL liquid-like clusters in solution increases local concentration in the focus, where the free motion and orientation of the clusters are strongly restricted, and the clusters show high rigidity and ordering. The cluster association and reorientation at the micrometer-sized focus is evolved to a large highly concentrated domain of the clusters, where the specific target crystal is grown. Initially, the high rigidity and ordering of the clusters strongly suppress the crystal grow rate compared to spontaneous crystal growth. Continuous laser trapping at the of the initially formed domain, however, leads to the transition to another domain with different concentration, rigidity, and ordering of the clusters, which surprisingly enhances the crystal growth rate. More interestingly, the clusters in both domains have anisotropic features reflecting the laser polarization direction, which also contributes to the crystal growth.Item type:Item, Laser-trapping assembling dynamics of molecules and proteins at surface and interface(2011) ;Masuhara, Hiroshi ;Sugiyama, Teruki ;Rungsimanon, Thitiporn ;Yuyama, Ken-ichiMiura, AtsushiLaser trapping of molecules and proteins in solution at room temperature is made possible by irradiating 1064-nm continuous-wave (CW) laser with power around 1 W. Although conventional small molecules are not trapped at the focal point, molecules that can form clusters upon assembling and proteins whose size is close to 10 nm are gathered, giving unique assembly structure. Glycine in H(2)O shows crystallization, urea in D(2)O gives a millimeter-sized giant droplet, and cobalt oxide-filled ferritin protein confirms assembly followed by precipitation. Solute concentration, solvent, and laser power are important factors for determining trapping and assembling phenomena, and the laser focal position is very critical. These unique behaviors are realized by setting the irradiation at the air/solution surface, inside the solution, and at the glass/solution interface. Laser trapping-induced crystallization, liquid/liquid phase separation, and precipitation are compared with the previous results and considered. After summarizing the results, we describe our future perspective and plans.Item type:Item, Rapid localized crystallization of lysozyme by laser trapping(2018-03-07) ;Yuyama, Ken-ichi ;Chang, Kai-Di ;Tu, Jing-Ru ;Masuhara, HiroshiSugiyama, TerukiConfining protein crystallization to a millimetre size was achieved within 0.5 h after stopping 1 h intense trapping laser irradiation, which shows excellent performance in spatial and temporal controllability compared to spontaneous nucleation. A continuous-wave near-infrared laser beam is tightly focused into a glass/solution interfacial layer of a supersaturated buffer solution of hen egg-white lysozyme (HEWL). The crystallization is not observed during laser trapping, but initiated by stopping the laser irradiation. The generated crystals are localized densely in a circular area with a diameter of a few millimetres around the focal spot and show specific directions of the optical axes of the HEWL crystals. To interpret this unique crystallization, we propose a mechanism that nucleation and the subsequent growth take place in a highly concentrated domain consisting of HEWL liquid-like clusters after turning off laser trapping.