Nucleic Acids Research Advance Access originally published online on October 22, 2008
Nucleic Acids Research 2009 37(Database issue):D374-D379; doi:10.1093/nar/gkn704
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Nucleic Acids Research, 2009, Vol. 37, Database issue D374-D379
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
This article appears in the following Nucleic Acids Research issue: Database issue [View the issue table of contents]
Articles |
SPROUTS: a database for the evaluation of protein stability upon point mutation
1Scientific Data Management Laboratory, Arizona State University, Tempe AZ 85282-5706, USA, 2Protein Structure Prediction, IMPMC, Université Paris 6, CNRS UMR 7590, 140 rue de Lourmel, 75015 Paris, France, 3Pharmaceutical Genomics Division, Translational Genomics Research Institute, 13400 E Shea Blvd, Scottsdale AZ 85259, USA and 4Laboratory of Genetics, Agricultural University of Athens, Iera Odos 75, 118 55 Athens, Greece
*To whom correspondence should be addressed. Tel: +1 480 727 6935; Fax: +1 480 965 8325; Email: zoe.lacroix{at}asu.edu
Received August 1, 2008. Revised September 26, 2008. Accepted September 29, 2008.
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.
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.