The Experts below are selected from a list of 249 Experts worldwide ranked by ideXlab platform
J. Dalrymple - One of the best experts on this subject based on the ideXlab platform.
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Structural characterisation of bis(Suberate) cobalt(II) 1.5 hydrate and a thermal analysis study of suberic acid and bis(Suberate) cobalt(II) 1.5 hydrate
Thermochimica Acta, 1993Co-Authors: J.r. Allan, J. DalrympleAbstract:Abstract A metal complex of suberic acid with cobalt of stoichiometry Co(C 8 H 12 O 4 ) · 1.5H 2 O has been prepared. The compound has a tetrahedral structure. Thermal decomposition studies of suberic acid and of Co(C 8 H 12 O 4 ) · 1.5H 2 O show that the suberic acid melts at 143°C, while the metal complex loses water and then the organic ligand, to give CO 3 O 4 .
Robert E. Blankenship - One of the best experts on this subject based on the ideXlab platform.
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Structural Analysis of the Homodimeric Reaction Center Complex from the Photosynthetic Green Sulfur Bacterium Chlorobaculum tepidum
2016Co-Authors: Hao Zhang, Jeremy D. King, Robert E. BlankenshipAbstract:ABSTRACT: The reaction center (RC) complex of the green sulfur bacterium Chlorobaculum tepidum is composed of the Fenna−Matthews− Olson antenna protein (FMO) and the reaction center core (RCC) complex. The RCC complex has four subunits: PscA, PscB, PscC, and PscD. We studied the FMO/RCC complex by chemically cross-linking the purified sample followed by biochemical and spectroscopic analysis. Blue-native gels showed that there were two types of FMO/RCC complexes, which are consistent with complexes with one copy of FMO per RCC and two copies of FMO per RCC. Sodium dodecyl sulfate−polyacrylamide gel electrophoresis analysis of the samples after cross-linking showed that all five subunits of the RC can be linked by three different cross-linkers: bissulfosuccinimidyl Suberate, disuccinimidyl Suberate, and 3,3-dithiobis-sulfosuccinimidyl propionate. The interaction sites of the cross-linked complex were also studied using liquid chromatography coupled to tandem mass spectrometry. The results indicated that FMO, PscB, PscD, and part of PscA are exposed on the cytoplasmic side of the membrane. PscD helps stabilize FMO to the reaction center and may facilitate transfer of the electro
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Structural Analysis of the Homodimeric Reaction Center Complex from the Photosynthetic Green Sulfur Bacterium Chlorobaculum tepidum
2015Co-Authors: Hao Zhang, Jeremy D. King, Robert E. BlankenshipAbstract:The reaction center (RC) complex of the green sulfur bacterium Chlorobaculum tepidum is composed of the Fenna–Matthews–Olson antenna protein (FMO) and the reaction center core (RCC) complex. The RCC complex has four subunits: PscA, PscB, PscC, and PscD. We studied the FMO/RCC complex by chemically cross-linking the purified sample followed by biochemical and spectroscopic analysis. Blue-native gels showed that there were two types of FMO/RCC complexes, which are consistent with complexes with one copy of FMO per RCC and two copies of FMO per RCC. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis of the samples after cross-linking showed that all five subunits of the RC can be linked by three different cross-linkers: bissulfosuccinimidyl Suberate, disuccinimidyl Suberate, and 3,3-dithiobis-sulfosuccinimidyl propionate. The interaction sites of the cross-linked complex were also studied using liquid chromatography coupled to tandem mass spectrometry. The results indicated that FMO, PscB, PscD, and part of PscA are exposed on the cytoplasmic side of the membrane. PscD helps stabilize FMO to the reaction center and may facilitate transfer of the electron from the RC to ferredoxin. The soluble domain of the heme-containing cytochrome subunit PscC and part of the core subunit PscA are located on the periplasmic side of the membrane. There is a close relationship between the periplasmic portions of PscA and PscC, which is needed for the efficient transfer of the electron between PscC and P840
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Structural analysis of the homodimeric reaction center complex from the photosynthetic green sulfur bacterium Chlorobaculum tepidum.
Biochemistry, 2014Co-Authors: Hao Zhang, Jeremy D. King, Robert E. BlankenshipAbstract:The reaction center (RC) complex of the green sulfur bacterium Chlorobaculum tepidum is composed of the Fenna–Matthews–Olson antenna protein (FMO) and the reaction center core (RCC) complex. The RCC complex has four subunits: PscA, PscB, PscC, and PscD. We studied the FMO/RCC complex by chemically cross-linking the purified sample followed by biochemical and spectroscopic analysis. Blue-native gels showed that there were two types of FMO/RCC complexes, which are consistent with complexes with one copy of FMO per RCC and two copies of FMO per RCC. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis of the samples after cross-linking showed that all five subunits of the RC can be linked by three different cross-linkers: bissulfosuccinimidyl Suberate, disuccinimidyl Suberate, and 3,3-dithiobis-sulfosuccinimidyl propionate. The interaction sites of the cross-linked complex were also studied using liquid chromatography coupled to tandem mass spectrometry. The results indicated that FMO, PscB, PscD, and part of PscA are exposed on the cytoplasmic side of the membrane. PscD helps stabilize FMO to the reaction center and may facilitate transfer of the electron from the RC to ferredoxin. The soluble domain of the heme-containing cytochrome subunit PscC and part of the core subunit PscA are located on the periplasmic side of the membrane. There is a close relationship between the periplasmic portions of PscA and PscC, which is needed for the efficient transfer of the electron between PscC and P840.
J.r. Allan - One of the best experts on this subject based on the ideXlab platform.
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Structural characterisation of bis(Suberate) cobalt(II) 1.5 hydrate and a thermal analysis study of suberic acid and bis(Suberate) cobalt(II) 1.5 hydrate
Thermochimica Acta, 1993Co-Authors: J.r. Allan, J. DalrympleAbstract:Abstract A metal complex of suberic acid with cobalt of stoichiometry Co(C 8 H 12 O 4 ) · 1.5H 2 O has been prepared. The compound has a tetrahedral structure. Thermal decomposition studies of suberic acid and of Co(C 8 H 12 O 4 ) · 1.5H 2 O show that the suberic acid melts at 143°C, while the metal complex loses water and then the organic ligand, to give CO 3 O 4 .
Hao Zhang - One of the best experts on this subject based on the ideXlab platform.
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Structural Analysis of the Homodimeric Reaction Center Complex from the Photosynthetic Green Sulfur Bacterium Chlorobaculum tepidum
2016Co-Authors: Hao Zhang, Jeremy D. King, Robert E. BlankenshipAbstract:ABSTRACT: The reaction center (RC) complex of the green sulfur bacterium Chlorobaculum tepidum is composed of the Fenna−Matthews− Olson antenna protein (FMO) and the reaction center core (RCC) complex. The RCC complex has four subunits: PscA, PscB, PscC, and PscD. We studied the FMO/RCC complex by chemically cross-linking the purified sample followed by biochemical and spectroscopic analysis. Blue-native gels showed that there were two types of FMO/RCC complexes, which are consistent with complexes with one copy of FMO per RCC and two copies of FMO per RCC. Sodium dodecyl sulfate−polyacrylamide gel electrophoresis analysis of the samples after cross-linking showed that all five subunits of the RC can be linked by three different cross-linkers: bissulfosuccinimidyl Suberate, disuccinimidyl Suberate, and 3,3-dithiobis-sulfosuccinimidyl propionate. The interaction sites of the cross-linked complex were also studied using liquid chromatography coupled to tandem mass spectrometry. The results indicated that FMO, PscB, PscD, and part of PscA are exposed on the cytoplasmic side of the membrane. PscD helps stabilize FMO to the reaction center and may facilitate transfer of the electro
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Structural Analysis of the Homodimeric Reaction Center Complex from the Photosynthetic Green Sulfur Bacterium Chlorobaculum tepidum
2015Co-Authors: Hao Zhang, Jeremy D. King, Robert E. BlankenshipAbstract:The reaction center (RC) complex of the green sulfur bacterium Chlorobaculum tepidum is composed of the Fenna–Matthews–Olson antenna protein (FMO) and the reaction center core (RCC) complex. The RCC complex has four subunits: PscA, PscB, PscC, and PscD. We studied the FMO/RCC complex by chemically cross-linking the purified sample followed by biochemical and spectroscopic analysis. Blue-native gels showed that there were two types of FMO/RCC complexes, which are consistent with complexes with one copy of FMO per RCC and two copies of FMO per RCC. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis of the samples after cross-linking showed that all five subunits of the RC can be linked by three different cross-linkers: bissulfosuccinimidyl Suberate, disuccinimidyl Suberate, and 3,3-dithiobis-sulfosuccinimidyl propionate. The interaction sites of the cross-linked complex were also studied using liquid chromatography coupled to tandem mass spectrometry. The results indicated that FMO, PscB, PscD, and part of PscA are exposed on the cytoplasmic side of the membrane. PscD helps stabilize FMO to the reaction center and may facilitate transfer of the electron from the RC to ferredoxin. The soluble domain of the heme-containing cytochrome subunit PscC and part of the core subunit PscA are located on the periplasmic side of the membrane. There is a close relationship between the periplasmic portions of PscA and PscC, which is needed for the efficient transfer of the electron between PscC and P840
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Structural analysis of the homodimeric reaction center complex from the photosynthetic green sulfur bacterium Chlorobaculum tepidum.
Biochemistry, 2014Co-Authors: Hao Zhang, Jeremy D. King, Robert E. BlankenshipAbstract:The reaction center (RC) complex of the green sulfur bacterium Chlorobaculum tepidum is composed of the Fenna–Matthews–Olson antenna protein (FMO) and the reaction center core (RCC) complex. The RCC complex has four subunits: PscA, PscB, PscC, and PscD. We studied the FMO/RCC complex by chemically cross-linking the purified sample followed by biochemical and spectroscopic analysis. Blue-native gels showed that there were two types of FMO/RCC complexes, which are consistent with complexes with one copy of FMO per RCC and two copies of FMO per RCC. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis of the samples after cross-linking showed that all five subunits of the RC can be linked by three different cross-linkers: bissulfosuccinimidyl Suberate, disuccinimidyl Suberate, and 3,3-dithiobis-sulfosuccinimidyl propionate. The interaction sites of the cross-linked complex were also studied using liquid chromatography coupled to tandem mass spectrometry. The results indicated that FMO, PscB, PscD, and part of PscA are exposed on the cytoplasmic side of the membrane. PscD helps stabilize FMO to the reaction center and may facilitate transfer of the electron from the RC to ferredoxin. The soluble domain of the heme-containing cytochrome subunit PscC and part of the core subunit PscA are located on the periplasmic side of the membrane. There is a close relationship between the periplasmic portions of PscA and PscC, which is needed for the efficient transfer of the electron between PscC and P840.
Zhaobin Qiu - One of the best experts on this subject based on the ideXlab platform.
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Crystallization Kinetics, Morphology, and Mechanical Properties of Novel Biodegradable Poly(ethylene succinate-co-ethylene Suberate) Copolyesters
Industrial & Engineering Chemistry Research, 2016Co-Authors: Shoutian Qiu, Zhaobin QiuAbstract:Through a two-step melt polycondensation method, three poly(ethylene succinate-co-ethylene Suberate) (PESSub) copolymers containing different contents of ethylene Suberate (ESub) from 4.8 to 15.3 mol % and with similar molecular weights were successfully synthesized in this research. To demonstrate the effect of the ESub composition, the crystallization kinetics, morphology, and mechanical properties of PESSub were systematically studied. The crystal structure of PESSub was the same as that of PES; however, with increasing ESub composition, the degree of crystallinity values slightly decreased. The increase of the ESub content led to a depression in the glass transition temperature, cold crystallization temperature, cold crystallization enthalpy, melting point, heat of fusion, and equilibrium melting point of PESSub. Increasing the ESub composition retained the crystallization mechanism but decreased the crystallization rates and spherulitic growth rates. The copolymers with higher ESub component showed g...
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Crystallization Kinetics, Morphology, and Mechanical Properties of Novel Biodegradable Poly(ethylene succinate-co-ethylene Suberate) Copolyesters
2016Co-Authors: Shoutian Qiu, Zhaobin QiuAbstract:Through a two-step melt polycondensation method, three poly(ethylene succinate-co-ethylene Suberate) (PESSub) copolymers containing different contents of ethylene Suberate (ESub) from 4.8 to 15.3 mol % and with similar molecular weights were successfully synthesized in this research. To demonstrate the effect of the ESub composition, the crystallization kinetics, morphology, and mechanical properties of PESSub were systematically studied. The crystal structure of PESSub was the same as that of PES; however, with increasing ESub composition, the degree of crystallinity values slightly decreased. The increase of the ESub content led to a depression in the glass transition temperature, cold crystallization temperature, cold crystallization enthalpy, melting point, heat of fusion, and equilibrium melting point of PESSub. Increasing the ESub composition retained the crystallization mechanism but decreased the crystallization rates and spherulitic growth rates. The copolymers with higher ESub component showed greater elongation at break but smaller tensile strength and Young’s modulus. The crystallization behavior and mechanical properties of the synthesized novel copolyesters were well-regulated by adjusting the content of the ESub units
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Crystallization kinetics and morphology of poly(ethylene Suberate)
Journal of Applied Polymer Science, 2015Co-Authors: Shoutian Qiu, Zhaobin QiuAbstract:The crystallization kinetics and morphology of poly(ethylene Suberate) (PESub) were studied in detail with differential scanning calorimetry, polarized optical microscopy, and wide-angle X-ray diffraction. The Avrami equation could describe the overall isothermal melt crystallization kinetics of PESub at different crystallization temperatures; moreover, the overall crystallization rate of PESub decreased with increasing crystallization temperature. The equilibrium melting point of PESub was determined to be 70.8°C. Ring-banded spherulites and a crystallization regime II to III transition were found for PESub. The Tobin equation could describe the nonisothermal melt crystallization kinetics of PESub at different cooling rates, while the Ozawa equation failed. © 2015 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2016, 133, 43086.
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Thermal properties and crystallization kinetics of poly(butylene Suberate)
Polymer, 2015Co-Authors: Zhiming Cui, Zhaobin QiuAbstract:Abstract In this work, we synthesized poly(butylene Suberate) (PBSub) with a weight average molecular weight of 3.64 × 104 g/mol from the monomers of butanediol and suberic acid via a two-step melt polycondensation method. The basic thermal behaviors, overall isothermal melt crystallization kinetics, crystal structure, spherulitic morphology and growth, thermal stability, and hydrolytic degradation of PBSub were systematically investigated for the first time. PBSub has a low glass transition temperature of about −61 °C, a melting point of 55.2 °C, and an equilibrium melting point of 61.4 °C. The overall isothermal melt crystallization kinetics of PBSub was investigated at different crystallization temperature values and analyzed by the Avrami equation. PBSub has an average Avrami exponent value of about 3, suggesting that the crystallization mechanism of PBSub may correspond to three-dimensional truncated sphere growth with athermal nucleation. An obvious spherulitic morphology was observed for PBSub, and the spherulitic growth rates decrease with increasing crystallization temperature. PBSub exhibits a crystallization regime II to regime III transition on the basis of the secondary nucleation theory. The crystal structure study reveals that PBSub is highly crystalline, presenting strong diffraction peaks and a great crystallinity of about 55%. The thermogravimetric analysis study demonstrates that PBSub has both a high decomposition temperature at 5 wt% weight loss of about 377 °C and a high temperature at the maximum degradation rate of about 421 °C, suggesting its good thermal stability. PBSub may undergo a hydrolytic degradation, which may be of interest for its end use as a degradable material in some special application fields.
