Resumen
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.
| Idioma original | Inglés |
|---|---|
| Páginas (desde-hasta) | 4959-4961 |
| Número de páginas | 3 |
| Publicación | Bioinformatics |
| Volumen | 38 |
| N.º | 21 |
| DOI | |
| Estado | Publicada - 1 nov. 2022 |
Huella
Profundice en los temas de investigación de 'CoDNaS-Q: a database of conformational diversity of the native state of proteins with quaternary structure'. En conjunto forman una huella única.Citar esto
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