CSSP-2.0: A refined consensus method for accurate protein secondary structure prediction.

ABSTRACT

Studying the relationship between sequences and their corresponding three-dimensional structure assists structural biologists in solving the protein-folding problem. Despite several experimental and in-silico approaches, still understanding or decoding the three-dimensional structures from the sequence remains a mystery. In such cases, the accuracy of the structure prediction plays an indispensable role. To address this issue, an updated web server (CSSP-2.0) has been created to improve the accuracy of our previous version of CSSP by deploying the existing algorithms. It uses input as probabilities and predicts the consensus for the secondary structure as a highly accurate three-state Q3 (helix, strand, and coil). This prediction is achieved using six recent top-performing methods: MUFOLD-SS, RaptorX, PSSpred v4, PSIPRED, JPred v4, and Porter 5.0. CSSP-2.0 validation includes datasets involving various protein classes from the PDB, CullPDB, and AlphaFold databases. Our results indicate a significant improvement in the accuracy of the consensus Q3 prediction. Using CSSP-2.0, crystallographers can sort out the stable regular secondary structures from the entire complex structure, which would aid in inferring the functional annotation of hypothetical proteins. The web server is freely available at https//bioserver3.physics.iisc.ac.in/cgi-bin/cssp-2/.