flDPnn: Accurate intrinsic disorder prediction with putative propensities of disorder functions

Identification of intrinsic disorder in proteins relies in large part on computational predictors, which demands that their accuracy should be high. Since intrinsic disorder carries out a broad range of cellular functions, it is desirable to couple the disorder and disorder function predictions. We...

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Veröffentlicht in:Nature communications 2021-07, Vol.12 (1), p.4438-4438, Article 4438
Hauptverfasser: Hu, Gang, Katuwawala, Akila, Wang, Kui, Wu, Zhonghua, Ghadermarzi, Sina, Gao, Jianzhao, Kurgan, Lukasz
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Sprache:eng
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Zusammenfassung:Identification of intrinsic disorder in proteins relies in large part on computational predictors, which demands that their accuracy should be high. Since intrinsic disorder carries out a broad range of cellular functions, it is desirable to couple the disorder and disorder function predictions. We report a computational tool, flDPnn, that provides accurate, fast and comprehensive disorder and disorder function predictions from protein sequences. The recent Critical Assessment of protein Intrinsic Disorder prediction (CAID) experiment and results on other test datasets demonstrate that flDPnn offers accurate predictions of disorder, fully disordered proteins and four common disorder functions. These predictions are substantially better than the results of the existing disorder predictors and methods that predict functions of disorder. Ablation tests reveal that the high predictive performance stems from innovative ways used in flDPnn to derive sequence profiles and encode inputs. flDPnn’s webserver is available at http://biomine.cs.vcu.edu/servers/flDPnn/ The authors present flDPnn, a computational tool for disorder and disorder function predictions from protein sequences. flDPnn was assessed with the data from the “Critical Assessment of Protein Intrinsic Disorder Prediction” experiment and on an independent and low-similarity test dataset, which show that flDPnn offers accurate predictions of disorder, fully disordered proteins and four common disorder functions.
ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-021-24773-7