Protein glycation locus identification method

Abstract

The invention provides a protein glycation locus identification method. The method comprises collecting protein glycation locus data, and extracting peptide chains which take lysine as the center fromthe protein glycation locus data to obtain a peptide chain sample set; encoding each amino acid of the peptide chain by adopting a single heat vector to obtain a peptide chain training set expressedby using the single heat vectors; training and producing an artificial peptide chain sample by using LSTM RNNs, and constructing an artificial peptide chain sample set; dividing each peptide chain inthe peptide chain sample set and the artificial peptide chain sample set into a series of biological words, and constructing features of peptide chains in the peptide chain sample set and the artificial peptide chain sample set through ProtVec based on the biological words; and obtaining a predictor based on CNN training, and identifying the protein glycation locus. According to the method of theinvention used to identify the protein glycation locus, feature extraction is less complex, and the accuracy of protein glycation locus identification is improved.

Description

technical field [0001] The present application relates to the technical field of protein function prediction, in particular to a method for identifying protein glycosylation sites. Background technique [0002] In 1912, LC Maillard first discovered and described the saccharification reaction. As one of the most important post-translational modification (Post-Translational Modifications, PTMs) process, the glycation reaction produces formyl or ketone groups with carbonyl groups through redox or peroxidation of sugars. The oxygen atom of the carbonyl group is negatively charged. Under high glucose conditions, non-enzymatic glycation reactions can occur with nucleophilic groups in proteins, DNA, lipids and other biomolecules to form Advanced Glycation End Products (AGEs). The long-term accumulation of AGEs in the human body will trigger two main cellular effects: (1) causing intermolecular bonding or cross-linking between extracellular and intracellular proteins, changing the ...

AI Technical Summary

Problems solved by technology

Although these methods have been developed to identify glycation sites, they suffer from low accuracy and overly complex feature extraction

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