Abstract

Secondary structure of proteins refers to local and repetitive conformations, such as α-helices and β-strands, which occur in protein structures. Computational prediction of secondary structure from protein sequences has a long history with three generations of predictive methods. This unit summarizes several recent third-generation predictors. We discuss their inputs and outputs, availability, and predictive performance and explain how to perform and interpret their predictions. We cover methods for the prediction of the 3-class secondary structure states (helix, strand, and coil) as well as the 8-class secondary structure states. Recent empirical assessments and our small-scale analysis reveal that these predictions are characterized by high levels of accuracy, between 70% and 80%. We emphasize that modern predictors are available to end users in the form of convenient-to-use Web servers and stand-alone software. © 2016 by John Wiley & Sons, Inc.

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