The RING 2.0 web server for high quality residue interaction networks
By Damiano Piovesan, Giovanni Minervini, Silvio C. E. Tosatto. Nucleic Acids Res., 2016
384 citations recorded by the source corpus.
Residue interaction networks (RINs) are an alternative way of representing protein structures where nodes are residues and arcs physico–chemical interactions. RINs have been extensively and successfully used for analysing mutation effects, protein folding, domain–domain communication and catalytic activity. Here we present RING 2.0, a new version of the RING software for the identification of covalent and non-covalent bonds in protein structures, including π–π stacking and π–cation interactions. RING 2.0 is extremely fast and generates both intra and inter-chain interactions including solvent and ligand atoms. The generated networks are very accurate and reliable thanks to a complex empirical re-parameterization of distance thresholds performed on the entire Protein Data Bank. By default, RING output is generated with optimal parameters but the web server provides an exhaustive interface to customize the calculation. The network can be visualized directly in the browser or in Cytoscape. Alternatively, the RING-Viz script for Pymol allows visualizing the interactions at atomic level in the structure. The web server and RING-Viz, together with an extensive help and tutorial, are available from URL: http://protein.bio.unipd.it/ring.
Subfields: Materials Chemistry, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/06f4e8bbe7ed9e4f997ee5015cd485789c3cf716
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In Materials Chemistry
- Zsuzsanna Dosztányi
- Bálint Mészáros
- Damiano Piovesan
- Michele Vendruscolo
- Silvio C. E. Tosatto
- Vladimir N Uversky
- Peter Tompa
- Carlo Camilloni
In Molecular Biology
- Zsuzsanna Dosztányi
- Bálint Mészáros
- Vladimir N Uversky
- Michele Vendruscolo
- Damiano Piovesan
- Silvio C. E. Tosatto
- Lukasz Kurgan
- Peter Tompa
Citations in the corpus
- MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins (2017, methodology): “Overview of tools used into MobiDB 3.0 Tool Type Description Mobi 2.0 Indirect Missing, high-temperature and mobile residues from PDB structures RING 2.0 Indirect Residue interactions from PDB structures, used to define LIPs RCI Indirect Random coil index from BMRB chemical shifts 2D Indirect Second”
- Impact of protein conformational diversity on AlphaFold predictions (2021, methodology): “Inter residue contacts have been obtained using the RING 2.0 web server [54].”