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Updated: Aug 28, 2025

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
Published on: July 16, 2017
CoDNaS-Q: a database of conformational diversity of the native state of proteins with quaternary structure
Nahuel Escobedo1,2, Ronaldo Romario Tunque Cahui3, Gastón Caruso1
1Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Buenos Aires B1876BXD, Argentina.
Summary:
A 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 Implementation:
CoDNaS-Q is freely accessible at http://ufq.unq.edu.ar/codnasq/ or https://codnas-q.bioinformatica.org/home. The data can be retrieved from the website. The source code of the database can be downloaded from https://github.com/SfrRonaldo/codnas-q.
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