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When two similar protein structures are compared, it is often difficult to analyse, or even identify, small differences, especially if the proteins are large. A method is described in which the refined coordinates of two nearly identical protein structures are compared by vector averaging of the differences in atomic coordinates over several consecutive residues. This technique detects regions of the protein where all the atoms move in the same direction. The magnitude and direction of the resultant average vector give the local conformational difference between the two structures. Regions with such correlated movements have been identified in several different protein structures.
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