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A Proposal of Pictures Sharing Network Using Multicast with NAK
Wataru UEMURA,Masashi MURATA 제어로봇시스템학회 2008 제어로봇시스템학회 국제학술대회 논문집 Vol.2008 No.10
At the wireless network, it is effective to decrease the packets in order to use the efficiency of the wireless band. We propose the multicast with NAK instead of the unicast in order to share the pictures which the cameras survillance system took at the parking lot.
Experimental validation of steering torque feedback simulator through vehicle running test
Taichi Shiiba,Wataru Murata 대한기계학회 2009 JOURNAL OF MECHANICAL SCIENCE AND TECHNOLOGY Vol.23 No.4
This paper describes a force feedback system based on real-time multibody dynamic analysis. This system can provide the analyzed reactive force to the operator through the operational device. In this study, this system is used as a steering torque feedback simulator of an automobile. This simulator can provide the haptic sensation of the steering wheel to the operator. For the purpose of evaluating the validity of the developed simulator, we conducted some vehicle running tests with an experimental electric vehicle. The results of these tests were compared with the results simulated on the steering torque feedback simulator. It was shown that the developed simulator can provide a suitable steering torque to the operator.
Effect of His 192 Mutation on the Activity of Alginate Lyase A1-III from Sphingomonas Species A1
YOON, HYE-JIN,CHOI, YONG-JIN,MIYAKE, OSAMU,HASHIMOTO, WATARU,MURATA, KOUSAKU,MIKAMI, BUNZO 한국미생물 · 생명공학회 2001 Journal of microbiology and biotechnology Vol.11 No.1
The alginate lyase A1-Ⅲ gene of Sphingomonas species A1 is composed of 1,077 nucleotides, encoding a protein (359 amino acids) with a molecular mass of 40,322Da. Recombinant A1-Ⅲ expressed in Escherichia coli exhibited the same full enzymatic activity as native A1-Ⅲ. In order to identify the critical residue for activity, a site-directed mutation was introduced into the A1-Ⅲ gene (H192A, His192→Ala). Recombinant A1-Ⅲ (H192A) exhibited a significant decrease in enzyme activity (one-thirty thousandth of that of A1-Ⅲ), without any conformational change, as detected by the CD spectra in the far UV region. Also, the chemical modification of wild-type Al-III with methyl 4-nitro benzene sulfonate resulted in a 40% decrease from the initial activity, whereas the same modification of A1-Ⅲ (H192A) produced no change in the activity. The role of His192 on the catalytic process was also explored based on a model of A1-Ⅲ docked with mannuronic acid into the active site.