Conditional Disorder, Ph, Sequence Analysis, Protein Structure, Bioinformatics
Digital Object Identifier (DOI)
Proteins are exposed to fluctuating environmental conditions in their cellular context and during their biotechnological production. Disordered regions are susceptible to these fluctuations and may experience solvent-dependent conformational switches that affect their local dynamism and activity. In a recent study, we modeled the influence of pH in the conformational state of IDPs by exploiting a charge–hydrophobicity diagram that considered the effect of solution pH on both variables. However, it was not possible to predict context-dependent transitions for multiple sequences, precluding proteome-wide analysis or the screening of collections of mutants. In this article, we present DispHScan, the first computational tool dedicated to predicting pH-induced disorder–order transitions in large protein datasets. The DispHScan web server allows the users to run pH-dependent disorder predictions of multiple sequences and identify context-dependent conformational transitions. It might provide new insights on the role of pH-modulated conditional disorder in the physiology and pathology of different organisms. The DispHScan web server is freely available for academic users, it is platform-independent and does not require previous registration.
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Citation / Publisher Attribution
Biomolecules, v. 11, issue 11, art. 1596
Scholar Commons Citation
Pintado-Grima, Carlos; Iglesias, Valentín; Santos, Jaime; Uversky, Vladimir N.; and Ventura, Salvador, "DispHScan: A Multi-Sequence Web Tool for Predicting Protein Disorder as a Function of pH" (2021). Molecular Medicine Faculty Publications. 915.