Nagoya Institute of Technology

About: Nagoya Institute of Technology is a education organization based out in Nagoya, Japan. It is known for research contribution in the topics: Thin film & Catalysis. The organization has 10766 authors who have published 19140 publications receiving 255696 citations. The organization is also known as: Nagoya Kōgyō Daigaku & Nitech.

On stability analysis of 2-D systems based on 2-D Lyapunov matrix inequalities

Abstract: A sufficient condition for the stability of two-dimensional (2-D) systems described in the Fornasin-Marchesini model is presented in a succinct form. The condition is expressed as a Lyapunov-like matrix inequality involved with the parallel addition of two positive definite matrices.

Light-induced structural changes of LOV domain-containing polypeptides from Arabidopsis phototropin 1 and 2 studied by small-angle X-ray scattering.

Abstract: Phototropin is a blue-light receptor of plants and comprises two light-receptive domains, LOV1 and LOV2, Ser/Thr kinase domain and one linker region connecting the LOV2 and the kinase domains. The LOV2 domain is thought to regulate predominantly the light-dependent autophosphorylation of the kinase domain, leading to cellular signaling cascades. In this study, we constructed recombinant LOV1, LOV2, and LOV2-linker polypeptides from phototropin 1 and phototropin 2 of Arabidopsis thaliana and studied their quaternary structures and light-dependent conformational changes by small-angle X-ray scattering. The molecular weights of the polypeptides determined from scattering intensities demonstrated the dimeric associations of LOV1 polypeptides of both isoforms. In contrast, while LOV2 and LOV2-linker polypeptides of phototropin 1 were homodimers, corresponding polypeptides of phototropin 2 existed as monomeric forms. Under blue-light irradiation, the LOV2-linker polypeptide of phototropin 1 displayed small but definite changes of the scattering profile. Through simulation of low-resolution molecular structures, the changes were likely explained as structural changes of the linker region and/or a movement of the region relative to the LOV2 domain. Light-induced profile changes were not observed in the Cys(512)Ala mutated LOV2-linker polypeptide of phototropin 1 losing the phototransformation capability. Thus, it was indicated that the photoreaction in the LOV2 domain probably caused the structural changes in the LOV2-linker polypeptide of phototropin 1. On the basis of the results, the interdomain interactions in phototropin are discussed.