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BioinformaticsBioinformaticsPeer-reviewed journal article

CoDNaS-Q: a database of conformational diversity of the native state of proteins with quaternary structure

Nahuel EscobedoiD, Ronaldo Romario Tunque CahuiiD, Gastón Caruso, Emilio García RíosiD, Layla HirshiD, Alexander Miguel MonzóniD, Gustavo D. ParisiiD, Nicolás PalópoliiD

PDFDOIPreprintCode

Abstract

SummaryA collection of conformers that exist in a dynamical equilibrium defines the native state of a protein. The structural differences between them describe their conformational diversity, a defining characteristic of the protein with an essential role in multiple cellular processes. Since most proteins carry out their functions by assembling into complexes, we have developed CoDNaS-Q, the first online resource to explore conformational diversity in homooligomeric proteins. It features a curated collection of redundant protein structures with known quaternary structure. CoDNaS-Q integrates relevant annotations that allow researchers to identify and explore the extent and possible reasons of conformational diversity in homooligomeric protein complexes. Availability and implementationCoDNaS-Q is freely accessible at http://ufq.unq.edu.ar/codnasq/. The data can be retrieved from the website. The source code of the database can be downloaded from https://github.com/SfrRonaldo/codnas-q. Contactnpalopoli@unq.edu.ar

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