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- 저자 : Hacioglu, Elise (검색결과 2 건)
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Load transportation by dual arm robot using sliding mode control
Nurkan Yagiz,Yuksel Hacioglu,Yunus Ziya Arslan 대한기계학회 2010 JOURNAL OF MECHANICAL SCIENCE AND TECHNOLOGY Vol.24 No.5
In this study, a sliding mode controlled dual arm robotic system was designed. Such multi-arm, collaborative and synchronous robots typically are employed in hazardous situations such as radioactive materials transport explosives disposal and industrial applications. In the present study, a high performance, robust, non-chattering sliding mode controller (SMC) was developed for the purpose of safe load handling, transportation and trajectory realization. First, dynamic equations of robot/load interaction were derived. Then, the robust SMC was designed for the dual arm robotic system. In order to test the robustness of the proposed SMC, parameter variations and external disturbances were introduced to the system. Furthermore, for comparative purposes, the conventional and widely used, PID controller was also applied to the dual arm robot. Significantly, it was found that the SMC made smaller trajectory tracking errors than the PID controller. An overall analysis of the numerical results confirmed that the dual-arm robotic systems with the proposed SMC can safely and effectively be used in hazardous applications.
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Le, Dung Tien,Lee, Byung Cheon,Marino, Stefano M.,Zhang, Yan,Fomenko, Dmitri E.,Kaya, Alaattin,Hacioglu, Elise,Kwak, Geun-Hee,Koc, Ahmet,Kim, Hwa-Young,Gladyshev, Vadim N. American Society for Biochemistry and Molecular Bi 2009 The Journal of biological chemistry Vol.284 No.7
<P>Methionine sulfoxide reductases (Msrs) are oxidoreductases that catalyze thiol-dependent reduction of oxidized methionines. MsrA and MsrB are the best known Msrs that repair methionine-S-sulfoxide (Met-S-SO) and methionine-R-sulfoxide (Met-R-SO) residues in proteins, respectively. In addition, an Escherichia coli enzyme specific for free Met-R-SO, designated fRMsr, was recently discovered. In this work, we carried out comparative genomic and experimental analyses to examine occurrence, evolution, and function of fRMsr. This protein is present in single copies and two mutually exclusive subtypes in about half of prokaryotes and unicellular eukaryotes but is missing in higher plants and animals. A Saccharomyces cerevisiae fRMsr homolog was found to reduce free Met-R-SO but not free Met-S-SO or dabsyl-Met-R-SO. fRMsr was responsible for growth of yeast cells on Met-R-SO, and the double fRMsr/MsrA mutant could not grow on a mixture of methionine sulfoxides. However, in the presence of methionine, even the triple fRMsr/MsrA/MsrB mutant was viable. In addition, fRMsr deletion strain showed an increased sensitivity to oxidative stress and a decreased life span, whereas overexpression of fRMsr conferred higher resistance to oxidants. Molecular modeling and cysteine residue targeting by thioredoxin pointed to Cys(101) as catalytic and Cys(125) as resolving residues in yeast fRMsr. These residues as well as a third Cys, resolving Cys(91), clustered in the structure, and each was required for the catalytic activity of the enzyme. The data show that fRMsr is the main enzyme responsible for the reduction of free Met-R-SO in S. cerevisiae.</P>
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