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Daniela Oelke (University of Konstanz, Konstanz, Germany)
In recent years the amount of protein sequence data has grown explosively, giving rise to many new research questions. One of those questions is what restrictions are protein sequences subjected to. More and more functionally equivalent variants of protein sequences are known. What do they have in common? What residue patterns would be acceptable to ensure a specific fold and a certain function? To address the above mentioned analysis questions, we developed VisAlign, a tool that combines the advantages of automatic calculations with an interactive visualization. The main component of the tool is an alignment viewer that becomes powerful by incorporating a flexible correlation measure. The parameters of the correlation measure can be interactively adapted to the needs of the analysis task. We display the calculated correlations by greying out all the columns which are not correlated with the selected basis column(s). This permits the user to easily grasp the results and perceive existing patterns. A 3D protein viewer allows localizing the position of the correlated columns within the protein structure. The tool has been successfully applied to the analysis of beta-lactamase sequenc