Document Type
Article
Publication Date
2021
Keywords
Conditional Disorder, Ph, Sequence Analysis, Protein Structure, Bioinformatics
Digital Object Identifier (DOI)
https://doi.org/10.3390/biom11111596
Abstract
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.
Rights Information
This work is licensed under a Creative Commons Attribution 4.0 License.
Was this content written or created while at USF?
Yes
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.
https://digitalcommons.usf.edu/mme_facpub/915
