Rafp-pred: Robust prediction of antifreeze proteins using localized analysis of n-peptide compositions

S Khan, I Naseem, R Togneri… - IEEE/ACM Transactions …, 2016 - ieeexplore.ieee.org
IEEE/ACM Transactions on Computational Biology and Bioinformatics, 2016ieeexplore.ieee.org
In extreme cold weather, living organisms produce Antifreeze Proteins (AFPs) to counter the
otherwise lethal intracellular formation of ice. Structures and sequences of various AFPs
exhibit a high degree of heterogeneity, consequently the prediction of the AFPs is
considered to be a challenging task. In this research, we propose to handle this arduous
manifold learning task using the notion of localized processing. In particular, an AFP
sequence is segmented into two sub-segments each of which is analyzed for amino acid …
In extreme cold weather, living organisms produce Antifreeze Proteins (AFPs) to counter the otherwise lethal intracellular formation of ice. Structures and sequences of various AFPs exhibit a high degree of heterogeneity, consequently the prediction of the AFPs is considered to be a challenging task. In this research, we propose to handle this arduous manifold learning task using the notion of localized processing. In particular, an AFP sequence is segmented into two sub-segments each of which is analyzed for amino acid and di-peptide compositions. We propose to use only the most significant features using the concept of information gain (IG) followed by a random forest classification approach. The proposed RAFP-Pred achieved an excellent performance on a number of standard datasets. We report a high Youden's index (sensitivity+specificity-1) value of 0.75 on the standard independent test data set outperforming the AFP-PseAAC, AFP_PSSM, AFP-Pred, and iAFP by a margin of 0.05, 0.06, 0.14, and 0.68, respectively. The verification rate on the UniProKB dataset is found to be 83.19 percent which is substantially superior to the 57.18 percent reported for the iAFP method.
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