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Self interacting proteins (SIPs) play an important role in various aspects of the structural and functional organization of the cell. Detecting SIPs is one of the most important issues in current molecular biology. Although a large number of SIPs data has been generated by experimental methods, wet laboratory approaches are both time-consuming and costly. In addition, they yield high false negative and positive rates. Thus, there is a great need for in silico methods to predict SIPs accurately and efficiently. In this study, a new sequence-based method is proposed to predict SIPs. The evolutionary information contained in Position-Specific Scoring Matrix (PSSM) is extracted from of protein with known sequence. Then, features are fed to an ensemble classifier to distinguish the self-interacting and non-self-interacting proteins. When performed on Saccharomyces cerevisiae and Human SIPs data sets, the proposed method can achieve high accuracies of 86.86 and 91.30 percent, respectively. Our method also shows a good performance when compared with the SVM classifier and previous methods. Consequently, the proposed method can be considered to be a novel promising tool to predict SIPs.

a b s t r a c tMicro liquid jetting technology is widely used in the field of electronic packaging. This paper presents a bond-graph model of a piezostack driven jetting dispenser that can dispense adhesive fluids accurately, rapidly, and flexibly. After describing the structural components and operating principles of the dispenser, the bond-graph model for the system is derived by integrating the electromechanical model with the fluid model. In the bond-graph model, the lumped parameter method is employed to obtain the conceptual bond-graph elements of the adhesive in the channels. Based on the proposed model, the jetting dispenser is designed and manufactured, and its performance is then evaluated through both computer simulations and experiments. Further simulation studies about the working properties based on the bond-graph model is carried out.

Protein-Protein Interactions (PPIs) play a vital role in most cellular processes. Although many efforts have been devoted to detecting protein interactions by high-throughput experiments, these methods are obviously expensive and tedious. Targeting these inevitable disadvantages, this study develops a novel computational method to predict PPIs using information on protein sequences, which is highly efficient and accurate. The improvement mainly comes from the use of the Rotation Forest (RF) classifier and the Local Phase Quantization (LPQ) descriptor from the Physicochemical Property Response (PR) Matrix of protein amino acids. When performed on three PPI datasets including Saccharomyces cerevisiae, Homo sapiens, and Helicobacter pylori, we obtained good results of average accuracies of 93.8%, 97.96%, and 89.47%, which are much better than in previous studies. Extensive validations have also been explored to evaluate the performance of the Rotation Forest ensemble classifier with the state-of-the-art Support Vector Machine classifier. These promising results indicate that the proposed method might play a complementary role for future proteomics research.

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