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RISS 인기검색어
- 검색키워드
- 저자 : Thamilselvan, Kamatchi (검색결과 4 건)
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Thamilselvan, Annadurai,Nesaraj, A Samson,Noel, Michael,James, E.J. The Korean Electrochemical Society 2015 Journal of electrochemical science and technology Vol.6 No.4
Capacitive deionization (CDI) process is a novel approach for desalination of an aqueous salt solution. In the present study, an activated carbon cloth (ACC) is proposed as effective electrode material. Initially the carbon cloth was activated in 1 M and 8 M HNO<sub>3</sub> for 9 hours at room temperature. The untreated and chemically activated carbon cloth (ACC) electrode materials were subjected to BET surface area measurements in order to get information about their specific surface area, average pore size, total pore volume and micropore area. The above materials were characterized by X-ray diffraction (XRD) and scanning electron microscope (SEM) also. The electrochemical studies for the electrodes were done using cyclic voltammetry (CV) in 0.1 M Na<sub>2</sub>SO<sub>4</sub> medium. From the studies, it was found that resistivity of the activated carbon cloth electrodes (treated in 1 M and 8 M HNO<sub>3</sub>) was decreased significantly by the chemical oxidation in nitric acid at room temperature and its capacitance was found to be 90 F/g (1 M HNO<sub>3</sub>) and 154 F/g (8 M HNO<sub>3</sub>) respectively in 0.1 M Na<sub>2</sub>SO<sub>4</sub> solution. The capacitive deionization behavior of a single cell CDI with activated carbon cloth electrodes was also studied and reported in this work.
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Regulation of Protein Structural Changes by Incorporation of a Small-Molecule Linker
Kim, Youngmin,Yang, Cheolhee,Kim, Tae Wu,Thamilselvan, Kamatchi,Kim, Yonggwan,Ihee, Hyotcherl MDPI 2018 INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES Vol.19 No.12
<P>Proteins have the potential to serve as nanomachines with well-controlled structural movements, and artificial control of their conformational changes is highly desirable for successful applications exploiting their dynamic structural characteristics. Here, we demonstrate an experimental approach for regulating the degree of conformational change in proteins by incorporating a small-molecule linker into a well-known photosensitive protein, photoactive yellow protein (PYP), which is sensitized by blue light and undergoes a photo-induced N-terminal protrusion coupled with chromophore-isomerization-triggered conformational changes. Specifically, we introduced thiol groups into specific sites of PYP through site-directed mutagenesis and then covalently conjugated a small-molecule linker into these sites, with the expectation that the linker is likely to constrain the structural changes associated with the attached positions. To investigate the structural dynamics of PYP incorporated with the small-molecule linker (SML-PYP), we employed the combination of small-angle X-ray scattering (SAXS), transient absorption (TA) spectroscopy and experiment-restrained rigid-body molecular dynamics (MD) simulation. Our results show that SML-PYP exhibits much reduced structural changes during photo-induced signaling as compared to wild-type PYP. This demonstrates that incorporating an external molecular linker can limit photo-induced structural dynamics of the protein and may be used as a strategy for fine control of protein structural dynamics in nanomachines.</P>
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Kim, Youngmin,Ganesan, Prabhakar,Jo, Junbeom,Kim, Seong Ok,Thamilselvan, Kamatchi,Ihee, Hyotcherl American Chemical Society 2018 The journal of physical chemistry. B, Condensed ma Vol.122 No.16
<P>Photoactive yellow protein (PYP) induces negative phototaxis in <I>Halorhodospira halophila</I> via photoactivation triggered by light-mediated chromophore isomerization. Chromophore isomerization proceeds via a volume-conserving isomerization mechanism due to the hydrogen-bond network and steric constraints inside the protein, and causes significant conformational changes accompanied by N-terminal protrusion. However, it is unclear how the structural change of the chromophore affects the remote N-terminal domain. To understand photocycle-related structural changes, we investigated the structural aspect of chromophore removal in PYP because it possesses a disrupted hydrogen-bond network similar to that in photocycle intermediates. A comparison of the structural aspects with those observed in the photocycle would give a clue related to the structural change mechanism in the photocycle<SUB>.</SUB> Chromophore removal effects were assessed via UV-vis spectroscopy, circular dichroism, and X-ray solution scattering. Molecular shape reconstruction and an experiment-restrained rigid-body molecular dynamics simulation based on the scattering data were performed to determine protein shape, size, and conformational changes upon PYP bleaching. Data show that chromophore removal disrupted the holo-PYP structure, resulting in a small N-terminal protrusion, but the extent of conformational changes was markedly less than those in the photocycle. This indicates that disruption of the hydrogen-bond network alone in bleached PYP does not induce the large conformational change observed in the photocycle, which thus must result from the organized structural transition around the chromophore triggered by chromophore photoisomerization along with disruption of the hydrogen-bond network between the chromophore and the PYP core.</P> [FIG OMISSION]</BR>
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