763 research outputs found

    SUMOhydro: A Novel Method for the Prediction of Sumoylation Sites Based on Hydrophobic Properties

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    Sumoylation is one of the most essential mechanisms of reversible protein post-translational modifications and is a crucial biochemical process in the regulation of a variety of important biological functions. Sumoylation is also closely involved in various human diseases. The accurate computational identification of sumoylation sites in protein sequences aids in experimental design and mechanistic research in cellular biology. In this study, we introduced amino acid hydrophobicity as a parameter into a traditional binary encoding scheme and developed a novel sumoylation site prediction tool termed SUMOhydro. With the assistance of a support vector machine, the proposed method was trained and tested using a stringent non-redundant sumoylation dataset. In a leave-one-out cross-validation, the proposed method yielded an excellent performance with a correlation coefficient, specificity, sensitivity and accuracy equal to 0.690, 98.6%, 71.1% and 97.5%, respectively. In addition, SUMOhydro has been benchmarked against previously described predictors based on an independent dataset, thereby suggesting that the introduction of hydrophobicity as an additional parameter could assist in the prediction of sumoylation sites. Currently, SUMOhydro is freely accessible at http://protein.cau.edu.cn/others/SUMOhydro/

    Ξ(1620)\Xi(1620) production in Kβˆ’pK^- p scattering process

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    In the present work, the production of Ξ(1620)\Xi(1620) in the Kβˆ’pK^- p scattering process is investigated by using an effective Lagrangian approach, where Ξ(1620)\Xi(1620) is considered as a KΛ‰Ξ›\bar{K} \Lambda molecular state. Our estimations indicate that the cross sections for Kβˆ’pβ†’K+Ξ(1620)βˆ’K^-p\to K^+ \Xi(1620)^- are (1.48βˆ’0.69+1.12)Β ΞΌb(1.48 ^{+ 1.12}_{-0.69}) \ \mathrm{\mu b} at PK=2.8Β GeVP_K=2.8 \ \mathrm{GeV}, where the uncertainties are resulted from the variation of the model parameter. As for the Kβˆ’pβ†’K+Ο€0Ξžβˆ’K^-p\to K^+ \pi^0 \Xi^- process, the cross sections are estimated to be (0.61βˆ’0.29+0.47)Β ΞΌb(0.61 ^{+0.47}_{-0.29})\ \mathrm{\mu b} at PK=2.8Β GeVP_K =2.8 \ \mathrm{GeV}, which is consistent with the experimental measurements.Comment: 5 pages, 5 figure

    Pionic and radiative transitions from Tcsˉ0+(2900)T_{c\bar{s}0}^+(2900) to Ds1+(2460)D_{s1}^+(2460) as a probe of the structure of Ds1+(2460)D_{s1}^+(2460)

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    In this work, we evaluated the widths of the pionic and radiative transitions from the Tcsˉ0+(2900)T_{c\bar{s}0}^{+}(2900) to the Ds1+(2460)D_{s1}^{+}(2460) in the Ds1+(2460)D_{s1}^{+}(2460) molecular frame and the Ds1+(2460)D_{s1}^{+}(2460) charmed-strange meson frame. Our estimations demonstrate that the transition widths in the Ds1+(2460)D_{s1}^{+}(2460) molecular frame are much larger than those in the the Ds1+(2460)D_{s1}^{+}(2460) charmed-strange meson frame. Specifically, the ratio of the widths of Γ(Tcsˉ0+(2900)→Ds1+π0)\Gamma(T_{c\bar{s}0}^{+}(2900)\to D_{s1}^{+} \pi^{0}) and Γ(Tcsˉ0+(2900)→D+(0)K0(+))\Gamma(T_{c\bar{s}0}^{+}(2900)\to D^{+(0)}K^{0(+)}) is estimated to be around 0.1 in the Ds1+(2460)D_{s1}^{+}(2460) charmed-strange meson frame, whereas the lower limit of this ratio is 0.67 in the Ds1+(2460)D_{s1}^{+}(2460) molecular frame. Thus, the aforementioned ratio could be employed as a tool for testing the nature of the Ds1+(2460)D_{s1}^{+}(2460).Comment: 8 pages, 7 figure
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