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1. Comparison of Sequence and Structure of Loop Regions in Lipases: Discovery of a Novel Mutable Domain | |||
Xu Yun,Shen Kunlong,Hu Suyuan,Wu Hongyi,Zhou Zhiliang,You Yuanming,Zhao Yi-Lei | |||
Biology 03 March 2014 | |||
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Abstract:Lipases (EC 3.1.1.3) possess two critical conformations, "open" and "close", during their catalytic process. The conformational changes, caused by the flexible loop regions in the enzymes, determine selectivity, regioselectivity and stereoselectivity of substrates in the enzymatic reactions. However, the principles beneath the phenomenon have not been clearly understood thoroughly yet, in terms of mutability on these loop regions. This paper employed both sequence and structure bioinformatical methods to study lipases available in database, especially for loop regions such as the 'lid' domain that was widely reported to connect substrate selectivity. Unsurprisingly, the 'lid' domain is quite mutable in a group of lipases which are in a moderate similarity for sequence and structure. However, we have found a more mutable, even the most mutable, domain among these loop regions. Loop 9, a very close to C terminus, is ranked top 1. The new discovery may rationalize the coupling effect from colipase. | |||
TO cite this article:Xu Yun,Shen Kunlong,Hu Suyuan, et al. Comparison of Sequence and Structure of Loop Regions in Lipases: Discovery of a Novel Mutable Domain[OL].[ 3 March 2014] http://en.paper.edu.cn/en_releasepaper/content/4587910 |
2. Thermal stability and unfolding pathways of Sso7d and its mutant F31A by molecular dynamics simulation | |||
Xu Xianjin,Wang Cunxin | |||
Biology 13 February 2012 | |||
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Abstract:The thermo-stability and unfolding behaviors of a small hyperthermophilic protein Sso7d as well as its single-point mutation F31A are studied by molecular dynamics simulation at temperatures of 300 K and 500 K. Simulations at 300 K show that the F31A mutant displays a much larger flexibility than the wild type, which implies that the mutation obviously decreases the protein’s stability. High temperature simulations at 500 K suggest that the unfolding of these two proteins evolves along different pathways. For the wild-type protein, the C-terminal alpha-helix is melted at the early unfolding stage, whereas it is destroyed much later in the unfolding process of the F31A mutant. Thus, the mutant unfolds faster than its parent protein. Besides, it is found that the triple-stranded antiparallel -sheet in the wild-type protein plays an important role in maintaining the stability of the entire structure. | |||
TO cite this article:Xu Xianjin,Wang Cunxin. Thermal stability and unfolding pathways of Sso7d and its mutant F31A by molecular dynamics simulation[OL].[13 February 2012] http://en.paper.edu.cn/en_releasepaper/content/4466109 |
3. The activity of myosin II motor and the volume of actin filament cooperatively regulate cytokinesis of | |||
Yang Fang,An Meiwen,Li Xiaona,Wang Li | |||
Biology 25 March 2010 | |||
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Abstract:The coordination of different cytoskeletons is an important factor in maintaining normal physiological and biochemical characteristics. In this study, normal rat kidney (NRK) cells in cytokinesis were treated with cytoskeleton inhibitors including cytochalasin D (CD), colchicine (COLC) oblebbistatin (myosin II motor activity inhibitor ). These inhibitors were released at the whole region and the localized region in two phases of cytokinesis. The influences were analyzed. It was showed that the roles of cytoskeleton inhibitors to cytokinesis were complex, for different treatment of inhibiotors corresponding to different results. The study indicated that the interaction in actin and the activity of myosin II motor is vital to cell shape and operation in every stages of cytokinesis. | |||
TO cite this article:Yang Fang,An Meiwen,Li Xiaona, et al. The activity of myosin II motor and the volume of actin filament cooperatively regulate cytokinesis of [OL].[25 March 2010] http://en.paper.edu.cn/en_releasepaper/content/41129 |
4. The conservative gene regulatory network in HK97 and λ phages | |||
Ai Duiyuan,Qi Yanjiao | |||
Biology 08 June 2009 | |||
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Abstract:Some conservative gene regulatory elements are found in Enterobacteria phage HK97 through sequences alignment, which are very similar to λ phage. Meanwhile, the regulated genes such as c1-gene, cro-gene, Q-gene, also show homology with λ phage. All of these results suggest hk97’s gene regulatory network is as same as λ phage. It implies this regulatory network is crucial and universal to lambda group. | |||
TO cite this article:Ai Duiyuan,Qi Yanjiao. The conservative gene regulatory network in HK97 and λ phages[OL].[ 8 June 2009] http://en.paper.edu.cn/en_releasepaper/content/32942 |
5. An improved predictive assay for radiotherapy to human hepatoma measured by prematurely chromosome condensation technique | |||
Yang Jianshe | |||
Biology 28 December 2005 | |||
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Abstract:To investigate the radiation response of hepatoma, SMMC-7721 cells were irradiated with 60Co γ-rays. Initial chromatid breaks were measured by counting the number of chromatid breaks and isochromatid breaks. A dose-dependent increase in radiation-induced chromatid/isochromatid breaks was observed in G1 and G2 phase respectively. A good relationship was found between cell survival and chromatin breaks. This study implied that low LET radiation-induced chromatid/isochromatid breaks can be possibly used as a good predictor of radiosensitivity of SMMC-7721 hepatoma cells. | |||
TO cite this article:Yang Jianshe. An improved predictive assay for radiotherapy to human hepatoma measured by prematurely chromosome condensation technique[OL].[28 December 2005] http://en.paper.edu.cn/en_releasepaper/content/4728 |
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