12/9/2014:
Paper: Ruben Acuña, Zoé Lacroix, Nikolaos Papandreou, and Jacques Chomilier. Protein intrachain contact prediction with most interacting residues (MIR). Bio-Algorithms and Med-Systems 10 (4), 227-242.
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The project SPROUTS (Structural Prediction for PRotein FOlding UTility System) was initiated in 2006 with the aim of compairing and integrating various structural analyses and producing a combined view of the results to the scientists. The first database compiled in 2008 presented data that capture representative folds and results related to the prediction of critical residues expected to belong to the folding nucleus of 429 structures produced by seven programs. The complexity required to manage seven different tools, the execution time, and the size of the results motivated the development of a database to organize the data and provide a meaningful interface to the scientist.
Originally, 10 structures corresponding to a total of 1211 amino acids had been processed by 5 different programs for the 19 possible mutations on each amino acid. Thus, the output data at the end of the experiment consisted in 115045 pieces of data. The execution of the different programs produced one file per amino acid for a total of more than 7200 files to manipulate. It was clear that this solution is