763 research outputs found
SUMOhydro: A Novel Method for the Prediction of Sumoylation Sites Based on Hydrophobic Properties
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/
production in scattering process
In the present work, the production of in the scattering
process is investigated by using an effective Lagrangian approach, where
is considered as a molecular state. Our
estimations indicate that the cross sections for are
at , where
the uncertainties are resulted from the variation of the model parameter. As
for the process, the cross sections are estimated to
be at ,
which is consistent with the experimental measurements.Comment: 5 pages, 5 figure
Pionic and radiative transitions from to as a probe of the structure of
In this work, we evaluated the widths of the pionic and radiative transitions
from the to the in the
molecular frame and the charmed-strange
meson frame. Our estimations demonstrate that the transition widths in the
molecular frame are much larger than those in the the
charmed-strange meson frame. Specifically, the ratio of the
widths of and
is estimated to be around
0.1 in the charmed-strange meson frame, whereas the lower
limit of this ratio is 0.67 in the molecular frame. Thus,
the aforementioned ratio could be employed as a tool for testing the nature of
the .Comment: 8 pages, 7 figure
Prediction of mucin-type O-glycosylation sites in mammalian proteins using the composition of k-spaced amino acid pairs
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