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. 2019 Jul 2;47(W1):W632-W635.
doi: 10.1093/nar/gkz407.

VOLPES: an interactive web-based tool for visualizing and comparing physicochemical properties of biological sequences

Affiliations

VOLPES: an interactive web-based tool for visualizing and comparing physicochemical properties of biological sequences

Lukas Bartonek et al. Nucleic Acids Res. .

Abstract

The structure, dynamics and, ultimately, biological function of proteins and nucleic acids are determined by the physicochemical properties of their primary sequences. Such properties are frequently captured via one-dimensional profile plots depicting a given physicochemical variable as a function of sequence position. Hydrophobicity, charge or structural disorder in proteins or nucleobase-density in nucleic acids are routinely visualized in this manner to analyze sequences at a glance. Such visualizations, however, are typically created case-by-case in a purely static manner, employ fixed visualization parameters only and do not enable a quantitative comparison between different sequences. Here, we present VOLPES (volpes.univie.ac.at), a user-friendly web server and the corresponding JavaScript library that enable a fully interactive, multifunctional visualization, analysis and comparison of the physicochemical properties of protein and nucleic-acid sequences, allowing unprecedented insight into biological sequence data and creating a starting point for further in-depth exploration.

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Figures

Figure 1.
Figure 1.
Example of a typical analysis performed via the VOLPES server: charge profiles calculated at different values of pH for a specified protein. A quantitative analysis of the similarity between profiles is given in the correlation matrix.

References

    1. Cuthbertson J.M., Doyle D.A., Sansom M.S.. Transmembrane helix prediction: a comparative evaluation and analysis. Protein Eng. Des. Sel. 2005; 18:295–308. - PubMed
    1. Snider C., Jayasinghe S., Hristova K., White S.H.. MPEx: a tool for exploring membrane proteins. Protein Sci. 2009; 18:2624–2628. - PMC - PubMed
    1. Deber C.M., Wang C., Liu L., Prior A.S., Agrawal S., Muskat B.L., Cuticchia A.J.. TM Finder: a prediction program for transmembrane protein segments using a combination of hydrophobicity and nonpolar phase helicity scales. Protein Sci. 2001; 10:212–219. - PMC - PubMed
    1. Zhao G., London E.. An amino acid “transmembrane tendency” scale that approaches the theoretical limit to accuracy for prediction of transmembrane helices: Relationship to biological hydrophobicity. Protein Sci. 2006; 15:1987–2001. - PMC - PubMed
    1. Das R.K., Pappu R.V.. Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues. Proc. Natl. Acad. Sci. U.S.A. 2013; 110:13392–13397. - PMC - PubMed

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