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With the explosion of protein sequences generated in the Post-Genomic Age, it is urgent to develop an automated method to predict protein quaternary structure. To explore this problem, we adopted an approach based on a sequence encoding descriptor by fusing PseAA (Pseudo Amino Acid) and DC (Dipeptide Composition) representing a protein sample. Here, a completely different approach, manifold learning...
Abstract-Prediction of protein-proteininteraction sites is very important to the function of a protein and drug design. In this paper, we adequately utilize the characters of ensemble learning, which can improve the accuracy of individual classifier and generalization ability of the system, and propose a new prediction method of protein-protein interaction sites: ensemble learning method based on...
Protein phosphorylation is a reversible post-translational modification commonly used by cell signaling networks to transmit information about the extracellular environment into intracellular organelles for the regulation of the activity and sorting of proteins within the cell. For this study we reconstructed a literature-based mammalian kinase-substrate network from several online resources. The...
One of the aims of the Protein Structure Initiative (PSI) in the post genome-sequencing era is to elucidate biochemical and biophysical functions of each protein structure. Thus, the development of new methods for a large-scale analysis/annotation of protein functional residues is inevitable. Currently existing methods are not capable to do so due to the lack of automation, availability, and/or poor...
Protein interaction domains play crucial roles in many complex cellular pathways. PDZ domains are one of the most common protein interaction domains. Prediction of binding specificity of PDZ domains by a computational manner could eliminate unnecessary, time-consuming experiments. In this study, interactions of PDZ domains are predicted by using a machine learning approach in which only primary sequences...
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