Abstract
Disordered proteins are highly abundant in regulatory processes such as transcription and cell-signaling. Different methods have been developed to predict protein disorder often focusing on different types of disordered regions. Here, we present MD, a novel META-Disorder prediction method that molds various sources of information predominantly obtained from orthogonal prediction methods, to significantly improve in performance over its constituents. In sustained cross-validation, MD not only outperforms its origins, but it also compares favorably to other state-of-the-art prediction methods in a variety of tests that we applied. Availability: http://www.rostlab.org/services/md/
Highlights
Disordered regions come in different flavors Many genes in higher organisms encode proteins or protein regions that do not adopt well-defined, stable three-dimensional (3D) structures under physiological conditions in isolation
We calculated the arithmetic average over the raw output of four disorder prediction methods: DISOPRED2 (Support Vector Machine based prediction of missing coordinates in Xray structures), IUPred, NORSnet and Ucon
Two extreme examples were contributed by the results of methods such as NORSnet and DISOPRED2 on the one side and IUPred and Ucon on the other side
Summary
Disordered regions come in different flavors Many genes in higher organisms encode proteins or protein regions that do not adopt well-defined, stable three-dimensional (3D) structures under physiological conditions in isolation. These proteins are commonly labeled as intrinsically disordered, unfolded, or natively unstructured proteins [1,2,3]. The assignment of disordered or unstructured regions is problematic, since by definition, these regions consist of an ensemble of rapidly inter-converting conformers that we cannot visualize. Since different experimental techniques capture different aspects or types of protein disorder, they occasionally do not agree on the assignments of these regions [7,8]. Results from this study suggested that unstructured regions in the cell are often protected from degradation by interaction with other molecules [8]
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