Abstract
In the biological systems, Acetylation is a crucial post-translational modification, prevalent in various physiological functions and pathological conditions like carcinoma and malignancies. To better understand serine acetylation, the first step is the efficient identification of the same. Although multiple large-scale in-vivo, ex-vivo, and in-vitro methods have been applied to detect serine acetylation biomarkers, these experimental methods are time-consuming and labor-intensive. This research aims to develop an in-silico solution to supplement wetlab experiments for efficient detection of serine acetylation sites by combining Chou’s Pseudo Amino Acid Composition (PseAAC) with deep neural networks (DNNs). By employing well-known DNNs for feature learning and classification of peptide sequences, our approach obsoletes the need to separately perform costly and cumbersome feature learning process. Based on performance evaluation using standard evaluation metrics, CNN and FCN based models, for AcetylSerine site identification, surpassed previously reported predictors which shows the efficacy of proposed approach.
Highlights
Acetylation is a reversible type of post-translational modification deemed important due to its effects on the metabolism of the body, genetic expressions and various disorders, i.e. carcinomas and malignancies, etc. [1]
True Positive (TP): Actual Aserine site forecasted via deep neural networks (DNNs) classifier as Aserine site
False Positive (FP): Actual non-Aserine site indicated via DNN classifier as Aserine site
Summary
Acetylation is a reversible type of post-translational modification deemed important due to its effects on the metabolism of the body, genetic expressions and various disorders, i.e. carcinomas and malignancies, etc. [1]. Acetylation is a reversible type of post-translational modification deemed important due to its effects on the metabolism of the body, genetic expressions and various disorders, i.e. carcinomas and malignancies, etc. The different reactions i.e. methylation, sulfation, hydration undergoes the conjugation process of the posttranslational modification but acetylation commonly takes place over the N-terminal (NH3+) group of the target residue of the histone core of the protein. The acetyl CoA usually acts as a donor of the target residue [4].
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