| dc.contributor.author |
Lonquety, M |
en |
| dc.contributor.author |
Lacroix, Z |
en |
| dc.contributor.author |
Papandreou, N |
en |
| dc.contributor.author |
Chomilier, J |
en |
| dc.date.accessioned |
2014-06-06T06:49:32Z |
|
| dc.date.available |
2014-06-06T06:49:32Z |
|
| dc.date.issued |
2009 |
en |
| dc.identifier.issn |
03051048 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1093/nar/gkn704 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/4658 |
|
| dc.subject.other |
article |
en |
| dc.subject.other |
computer prediction |
en |
| dc.subject.other |
energy |
en |
| dc.subject.other |
information processing |
en |
| dc.subject.other |
point mutation |
en |
| dc.subject.other |
priority journal |
en |
| dc.subject.other |
protein database |
en |
| dc.subject.other |
protein folding |
en |
| dc.subject.other |
protein stability |
en |
| dc.subject.other |
protein structure |
en |
| dc.subject.other |
Structural Prediction for pRotein fOlding UTility System |
en |
| dc.subject.other |
structural proteomics |
en |
| dc.subject.other |
structure analysis |
en |
| dc.subject.other |
Computer Graphics |
en |
| dc.subject.other |
Databases, Protein |
en |
| dc.subject.other |
Point Mutation |
en |
| dc.subject.other |
Protein Conformation |
en |
| dc.subject.other |
Protein Folding |
en |
| dc.subject.other |
Protein Stability |
en |
| dc.subject.other |
Proteins |
en |
| dc.title |
SPROUTS: A database for the evaluation of protein stability upon point mutation |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1093/nar/gkn704 |
en |
| heal.publicationDate |
2009 |
en |
| heal.abstract |
SPROUTS (Structural Prediction for pRotein fOlding UTility System) is a new database that provides access to various structural data sets and integrated functionalities not yet available to the community. The originality of the SPROUTS database is the ability to gain access to a variety of structural analyses at one place and with a strong interaction between them. SPROUTS currently combines data pertaining to 429 structures that capture representative folds and results related to the prediction of critical residues expected to belong to the folding nucleus: the MIR (Most Interacting Residues), the description of the structures in terms of modular fragments: the TEF (Tightened End Fragments), and the calculation at each position of the free energy change gradient upon mutation by one of the 19 amino acids. All database results can be displayed and downloaded in textual files and Excel spreadsheets and visualized on the protein structure. SPROUTS is a unique resource to access as well as visualize state-of-the-art characteristics of protein folding and analyse the effect of point mutations on protein structure. It is available at http://bioinformatics.eas.asu.edu/sprouts.html. © 2008 The Author(s). |
en |
| heal.journalName |
Nucleic Acids Research |
en |
| dc.identifier.issue |
SUPPL. 1 |
en |
| dc.identifier.volume |
37 |
en |
| dc.identifier.doi |
10.1093/nar/gkn704 |
en |
| dc.identifier.spage |
D374 |
en |
| dc.identifier.epage |
D379 |
en |