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ABSTRACT: Background
Prediction of protein structural classes (alpha, beta, alpha + beta and alpha/beta) from amino acid sequences is of great importance, as it is beneficial to study protein function, regulation and interactions. Many methods have been developed for high-homology protein sequences, and the prediction accuracies can achieve up to 90%. However, for low-homology sequences whose average pairwise sequence identity lies between 20% and 40%, they perform relatively poorly, yielding the prediction accuracy often below 60%.Results
We propose a new method to predict protein structural classes on the basis of features extracted from the predicted secondary structures of proteins rather than directly from their amino acid sequences. It first uses PSIPRED to predict the secondar
SUBMITTER: Yang JY
PROVIDER: S-EPMC3009544 | biostudies-literature | 2010 Jan
REPOSITORIES: biostudies-literature