Abstract
The structure of protein gains additional stability against various detrimental effects by the presence of disulfide bonds. The formation of correct disulfide bonds between cysteine residues ensures proper in vivo and in vitro folding of the protein. Many cysteine residues can be present in the polypeptide chain of a protein, however, not all cysteine residues are involved in the formation of a disulfide bond, and therefore, accurate prediction of these bonds is crucial for identifying biophysical characteristics of a protein. In the present study, a novel method is proposed for the prediction of intramolecular disulfide bonds accurately using statistical moments and PseAAC. The pSSbond-PseAAC uses PseAAC along with position and composition relative features to calculate statistical moments. Statistical moments are important as they are very sensitive regarding the position of data sequences and for prediction of intramolecular disulfide bonds, moments are combined together to train neural networks. The overall accuracy of the pSSbond-PseAAC is 98.97% to sensitivity value 98.92%, specificity 98.99% and 0.98 MCC; and it outperforms various previously reported studies.
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