Publications by authors named "Nozomi Arai"

Hypothesis: The formation of soft colloidal crystals, which are nonclose-packed ordered arrays of colloidal particles suspended in a solvent, is dictated by a single physical factor that yields a fixed threshold at order-disorder boundaries for different experimental conditions such as ion concentration, solvent type, and particle size. Identifying the determinant factor and its threshold value should enable the prediction of the critical concentrations of colloidal particles to form soft colloidal crystals.

Experiments: Soft colloidal crystals were fabricated using a series of monohydric alcohols as dispersion media and reflectance spectra were measured to locate order-disorder boundaries.

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The attachment of solid particles to the surface of immersed gas bubbles plays a fundamental role in surface science, and hence plays key roles in various engineering fields ranging from industrial separation processes to the fabrication of functional materials. However, detailed investigation from a microscopic view on how a single particle attaches to a bubble surface and how the particle properties affect the attachment behavior has been so far scarcely addressed. Here, we observed the attachment of a single particle to a bubble surface using a high-speed camera and systematically investigated the effects of the wettability and shape of particles.

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While the currently available techniques for the self-assembly of colloidal particles show great promise owing to their simplicity and high efficiency, they are plagued by the fact that they result in colloidal crystals with defects. Here, in order to overcome this problem, we propose a strategy that uses a suspension of nanoparticles (i.e.

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Background: The purpose of this study was to evaluate the validity of the PATHFAST fertility marker assays for the rapid measurement of female hormones including: LH, FSH, Estradiol (E2), Progesterone (P4), Prolactin (PRL), and HCG. As for the PATHFAST fertility marker assays, female hormones can be measured by whole blood, plasma, and serum.

Methods: The correlation of the heparin whole blood and the plasma samples in the PATHFAST was examined.

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Zinc finger fusion proteins, having a Ca-binding site from troponin C, were created to develop Ca-responsive regulation of DNA binding. The typical zinc finger folding of a novel fusion protein with a single finger, F2-Tn, was investigated using UV-vis spectroscopy of the Co-substituted form and CD experiments. Detailed structural analyses of F2-Tn/Zn2+ using NMR experiments and structural calculations clarify that our fusion protein gives a native zinc finger folding with the artificial Ca-binding domain intervening two helices.

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