Biology:Database of protein conformational diversity
 | |
|---|---|
| Content | |
| Description | Protein conformational diversity. |
| Contact | |
| Research centre | Universidad Nacional de Quilmes |
| Laboratory | Centro de Estudios e Investigaciones |
| Author(s) | Ezequiel I Juritz |
| Primary citation | Juritz & al. (2011)[1] |
| Release date | 2010 |
| Access | |
| Website | http://www.pcdb.unq.edu.ar |
The Database of protein conformational diversity (PCDB) is a database of diversity of protein tertiary structures within protein domains as determined by X-ray crystallography.[1][2] Proteins are inherently flexible and this database collects information on this subject for use in molecular research. It uses the CATH database as a source of structures for each protein and reports the range of differences in the structures based on their superposition and reports a maximum RMSD. The interface for the database allows researchers to find proteins with a range of conformational flexibility allowing them to find highly flexible proteins for example. The database is run and maintained by a group of researchers based at the Universidad Nacional de Quilmes in Argentina.[citation needed]
See also
References
- ↑ 1.0 1.1 "PCDB: a database of protein conformational diversity". Nucleic Acids Res. 39 (Database issue): D475–9. January 2011. doi:10.1093/nar/gkq1181. PMID 21097895.
- ↑ "The 2011 Nucleic Acids Research Database Issue and the online Molecular Biology Database Collection". Nucleic Acids Res. 39 (Database issue): D1–6. January 2011. doi:10.1093/nar/gkq1243. PMID 21177655.
External links
- "Protein Conformational Database". Structural Bioinformatics Group; National University of Quilmes. Archived from the original on 2012-03-30. https://web.archive.org/web/20120330231747/http://74.54.147.134/~ezepcdb3/. Retrieved 2011-08-19.
 |  |
