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Colin Combe; Salman Tahir; Lutz Fischer; Zhuo Angel Chen; Juan Zou; Adam Belsom; Lauri Peil; Jimi-Carlo Bukowski-Wills; Juri Rappsilber (Wellcome Trust Centre for Cell Biology, King's Buildings, University of Edinburgh, Mayfield Road, Edinburgh, Scotland EH9 3JR )
Cross-linking/MS acquires information on the physical structure of proteins and on protein-protein interactions. Cross-linkers are short molecules, the ends of which react with certain amino acids. Mass spectrometry is then used to identify the cross-linked amino acids in the context of protein fragments (peptides). As the maximum length of the cross-link is known this data provides proximity information for the two amino acids. The protein proximity information is at a resolution unavailable from other sources and it can provide a unique perspective on the arrangement of proteins in complexes and on conformational changes within protein complexes. The data is an invaluable input to both modelling the physical structure of proteins and investigating the functional relationships between them. The data forms a network of cross-links. The visualisation shows the topology of this network as a hierarchical graph; links between proteins are shown but the nodes can be expanded to show (inter and intra protein) cross-links between individual amino acids.