TANGO
TANGO is a statistical mechanics algorithm to predict protein aggregation. It was developed by Luis Serrano's group at EMBL in Heidelberg, Germany, together with Joost Schymkowitz and Frederic Rousseau of VIB's SWITCH laboratory in Brussels, Belgium, during the time they were working at EMBL.
TANGO is based on the physico-chemical principles of b-sheet formation extended by the assumption that the core regions of an aggregate are fully buried. The TANGO algorithm accurately predicts the aggregation of a dataset of 179 peptides from 21 different proteins as well as of a new set of 71 peptides derived from disease-related human proteins (prion protein, lysozyme and b2-microglobulin) as measured in our laboratories in VIB & EMBL. TANGO also correctly predicts pathogenic as well as protective mutations of the Alzheimer's b-peptide, human lysozyme and transthyrethin, and discriminates between b-sheet tendency and aggregation. The success of TANGO confirms the model of intermolecular b-sheet formation as a wide-spread underlying mechanism of protein aggregation. Furthermore, the algorithm opens the way to a fully automated, sequence based design strategy to improve aggregation properties of proteins of scientific or industrial interest.
Click here to be relocated to TANGO application at the EMBL website.
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