pSSbond-PseAAC: Prediction of disulfide bonding sites by integration of PseAAC and statistical moments.

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.