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| Content | |
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| Description | conformational dynamics of proteins and supramolecular protein assemblies. |
| Contact | |
| Primary citation | PMID 21051356 |
| Release date | 2010 |
| Access | |
| Website | http://www.cdyn.org |
The conformational dynamics data bank (CDDB) is a database about conformational dynamics of heavy proteins and protein assemblies. The CDDB is useful when used alongside static structural data to aid research into protein function. It is also helpful in identifying protein assemblies that are essential to cell function. [1]
Analysis is carried out by coarse-grained computation of the structures present in the electron microscopy data bank (EMDB). This analysis shows equilibrium thermal fluctuations and elastic strain energy distributions, which allows for identification of rigid and flexible protein domains. The results also provide information on correlations in molecular motions which can be used to identify molecular regions that are highly coupled dynamically. [1]
References
- ^ a b Kim, Do-Nyun; Altschuler Josiah; Strong Campbell; McGill Gaël; Bathe Mark (Jan 2011). "Conformational dynamics data bank: a database for conformational dynamics of proteins and supramolecular protein assemblies". Nucleic Acids Res. 39 (Database issue). England: D451-5. doi: 10.1093/nar/gkq1088. PMC 3013685. PMID 21051356.
External links
 | This Biological database-related article is a stub. You can help Wikipedia by expanding it. |
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| |
| Content | |
|---|---|
| Description | conformational dynamics of proteins and supramolecular protein assemblies. |
| Contact | |
| Primary citation | PMID 21051356 |
| Release date | 2010 |
| Access | |
| Website | http://www.cdyn.org |
The conformational dynamics data bank (CDDB) is a database about conformational dynamics of heavy proteins and protein assemblies. The CDDB is useful when used alongside static structural data to aid research into protein function. It is also helpful in identifying protein assemblies that are essential to cell function. [1]
Analysis is carried out by coarse-grained computation of the structures present in the electron microscopy data bank (EMDB). This analysis shows equilibrium thermal fluctuations and elastic strain energy distributions, which allows for identification of rigid and flexible protein domains. The results also provide information on correlations in molecular motions which can be used to identify molecular regions that are highly coupled dynamically. [1]
References
- ^ a b Kim, Do-Nyun; Altschuler Josiah; Strong Campbell; McGill Gaël; Bathe Mark (Jan 2011). "Conformational dynamics data bank: a database for conformational dynamics of proteins and supramolecular protein assemblies". Nucleic Acids Res. 39 (Database issue). England: D451-5. doi: 10.1093/nar/gkq1088. PMC 3013685. PMID 21051356.
External links
|
| This Biological database-related article is a stub. You can help Wikipedia by expanding it. |