| URL: | http://www.dsimb.inserm.fr/dsimb_tools/polyproline/ |
| Full name: | |
| Description: | PolyprOnline database is, therefore, dedicated to PPII structure assignment and analysis to facilitate the study of PPII structure and functional roles. |
| Year founded: | 2014 |
| Last update: | 2014-10-07 |
| Version: | v1.0 |
| Accessibility: |
Accessible
|
| Country/Region: | France |
| Data type: | |
| Data object: |
NA
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| Database category: | |
| Major species: |
NA
|
| Keywords: |
| University/Institution: | French National Institute of Health and Medical Research |
| Address: | U1134, Paris, France |
| City: | Paris |
| Province/State: | |
| Country/Region: | France |
| Contact name (PI/Team): | Jean-Christophe Gelly |
| Contact email (PI/Helpdesk): | jean-christophe.gelly@univ-paris-diderot.fr |
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PolyprOnline: polyproline helix II and secondary structure assignment database. [PMID: 25380779]
The polyproline helix type II (PPII) is a regular protein secondary structure with remarkable features. Many studies have highlighted different crucial biological roles supported by this local conformation, e.g. in the interactions between biological macromolecules. Although PPII is less frequently present than regular secondary structures such as canonical alpha helices and beta strands, it corresponds to 3-10% of residues. Up to now, PPII is not assigned by most popular assignment tools, and therefore, remains insufficiently studied. PolyprOnline database is, therefore, dedicated to PPII structure assignment and analysis to facilitate the study of PPII structure and functional roles. This database is freely accessible from www.dsimb.inserm.fr/dsimb_tools/polyproline. © The Author(s) 2014. Published by Oxford University Press. |