SPROUTS: a database for the evaluation of protein stability upon point mutation
By Mathieu Lonquety, Zoé Lacroix, Nikolaos Papandreou, Jacques Chomilier. 2008
28 citations recorded by the source corpus.
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.
Subfields: Materials Chemistry, Molecular Biology
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Materials Chemistry
- Martin Weigt
- Dan S. Tawfik
- Nobuhiko Tokuriki
- Alexander Schug
- O. Tenaillon
- Matteo Figliuzzi
- H. Jacquier
In Molecular Biology
- Martin Weigt
- Matteo Figliuzzi
- Alexander Schug
- Dan S. Tawfik
- Nobuhiko Tokuriki
- H. Jacquier
- O. Tenaillon
- Anne-Florence Bitbol
Citations in the corpus
- Coevolutionary Landscape Inference and the Context-Dependence of Mutations in Beta-Lactamase TEM-1 (2015, methodology): “coli TEM-1 protein point mutations for the web-based programs mentioned in the article have been downloaded from the SPROUTS database [27].”
- Stability effects of mutations and protein evolvability. (2009, background): “The combination of both has also been explored [19,25,26 ,27].”