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bioRxiv · 10.1101/2022.02.15.480082

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

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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BibTeXRIS

Escobedo, N., Tunque Cahui, R. R., Caruso, G., Garcia Rios, E., Hirsh, L., Monzon, A. M., Parisi, G., Palopoli, N.. 2022-02-19. CoDNaS-Q: a database of conformational diversity of the native state of proteins with quaternary structure. https://doi.org/10.1101/2022.02.15.480082

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