Abstract

Calpains are an important family of the Ca2+-dependent cysteine proteases which catalyze the limited proteolysis of many specific substrates. Calpains play crucial roles in basic physiological and pathological processes, and identification of the calpain cleavage sites may facilitate the understanding of the molecular mechanisms and biological function. But traditional experiment approaches to predict the sites are accurate, and are always labor-intensive and time-consuming. Thus, it is common to see that computational methods receive increasing attention due to their convenience and fast speed in recent years. In this study, we develop a new predictor based on the support vector machine (SVM) with the maximum relevance minimum redundancy (mRMR) method followed by incremental feature selection (IFS). And we concern the feature of physicochemical/biochemical properties, sequence conservation, residual disorder, secondary structure, and solvent accessibility to represent the calpain cleavage sites. Experimental results show that the performance of our predictor is better than several other state-of- the-art predictors, whose average prediction accuracy is 79.49%, sensitivity is 62.31%, and specificity is 88.12%. Since user-friendly and publicly accessible web servers represent the future direction for developing practically more useful predictors, here we have provided a web-server for the method presented in this paper.

Highlights

  • Calpains are an important family of the Ca2+-dependent cysteine proteases which catalyze the limited proteolysis of many specific substrates

  • We develop a new predictor based on the support vector machine (SVM) with the maximum relevance minimum redundancy method followed by incremental feature selection (IFS)

  • Calpains are an important family of the Ca2+-dependent cysteine proteases which catalyze the limited proteolysis of many specific substrates [1, 2]

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Summary

Introduction

Calpains are an important family of the Ca2+-dependent cysteine proteases which catalyze the limited proteolysis of many specific substrates [1, 2]. 16 known calpain isoform genes are founded in humans. Calpains play crucial roles in basic physiological and pathological processes, including the regulation of gene expression, signal transduction, cell death and apoptosis, remodeling cytoskeletal attachments during cell fusion or motility, and cell cycle progression [3,4,5]. Traditional experimental identification and characterization of calpain cleavage sites are laborintensive and expensive. Calpain cleavage sites prediction attracts more and more attention, and more and more studies have understood its regulatory roles and molecular mechanisms of calpain cleavage

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