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The ModFOLD4 server for the quality assessment of 3D protein models
Author(s) -
Liam J. McGuffin,
Maria T. Buenavista,
Daniel B. Roche
Publication year - 2013
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/gkt294
Subject(s) - biology , quality (philosophy) , protein tertiary structure , web server , similarity (geometry) , computer science , computational biology , bioinformatics , artificial intelligence , the internet , operating system , biochemistry , philosophy , epistemology , image (mathematics)
Once you have generated a 3D model of a protein, how do you know whether it bears any resemblance to the actual structure? To determine the usefulness of 3D models of proteins, they must be assessed in terms of their quality by methods that predict their similarity to the native structure. The ModFOLD4 server is the latest version of our leading independent server for the estimation of both the global and local (per-residue) quality of 3D protein models. The server produces both machine readable and graphical output, providing users with intuitive visual reports on the quality of predicted protein tertiary structures. The ModFOLD4 server is freely available to all at: http://www.reading.ac.uk/bioinf/ModFOLD/.

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