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Stephen Todd, Peter Todd, Frederic Fol Leymarie, William Latham, Jim Hughes, Stephen Taylor (Goldsmiths, University of London, U.K.; University of Oxford, U.K.)
FoldSynth (1.0) was designed to interactively study protein folding. Recently we started to apply and further develop it to better understand the 3D topology that results from interactions in the genome. This helps scientists understand the Topologically Associated Domains (TADs). FoldSynth reads contact probability data which are used to create 'springs', which in turn drive the dynamics to find possible 3D conformations. We can annotate interactively a 2D distance matrix or the associated 3D molecular view coloured by the structure information contained in BED (Browser Extensible Data) files. We can also read and integrate WIG (wiggle format) files which show numerical information of other assays across the genome and use these to annotate the 2D matrix and change the 3D view. Each particle represents a window of 5,000 residues giving over 18,000 particles with over 7 million recorded contact probabilities. FoldSynth can operate on a small segment or pair of segments at a time while the entire dataset is loaded for greater fluidity. The segment choice can be made in a companion custom built Large Matrix Viewer (LMV) that shows the distance matrix at multiple zoom levels.