EasyModel: a user-friendly web-based interface based on MODELLER.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
11 10 2023
Historique:
received: 06 06 2023
accepted: 09 10 2023
medline: 2 11 2023
pubmed: 12 10 2023
entrez: 11 10 2023
Statut: epublish

Résumé

Three-dimensional protein structures are invaluable sources of information for the functional annotation of protein molecules. Describing the function of a protein sequence is one of the most common problems in biology. Generally, this problem can be facilitated by studying the tertiary structure of proteins. In the lack of protein structures, comparative modeling often provides a useful three-dimensional model of the protein associated with at least one known protein structure. Comparative modeling predicts the tertiary structure of a certain protein sequence (target) mainly based on its homological sequence to the sequence of one or more proteins with known structures (templates). MODELLER is one of the most widely used tools for homology or comparative modeling of three-dimensional protein structures. However, most users find it challenging to start with MODELLER as it is a command line based and requires knowledge of basic Python scripting to use it efficiently. In this study, a web-based interface has been designed to predict the tertiary structure of proteins based on Modeller, which does the comparative modeling automatically, and uses PHP and Python programming languages. This tool is called "EasyModel" and is available at http://bioinf.modares.ac.ir/software/easymodel/ . EasyModel provides a straightforward graphical interface for Modeller that can be used in only one browser.

Identifiants

pubmed: 37821634
doi: 10.1038/s41598-023-44505-9
pii: 10.1038/s41598-023-44505-9
pmc: PMC10567746
doi:

Substances chimiques

Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

17185

Informations de copyright

© 2023. Springer Nature Limited.

Références

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Auteurs

Seyed Shahriar Arab (SS)

Department of Biophysics, Faculty of Biological Sciences, Tarbiat Modares University, 1411713116, Terhan, Iran. sh.arab@modares.ac.ir.

Alireza Dantism (A)

Department of Biophysics, Faculty of Biological Sciences, Tarbiat Modares University, 1411713116, Terhan, Iran.

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Classifications MeSH