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Purification of cloned trypanosomal calmodulin and preliminary NMR studies
P J Sweeney1, J M Walker, D G Reid
1Division of Biological Sciences, Hatfield Polytechnic, Hertfordshire, U.K.
Journal of Chromatography
|February 22, 1991
Abstract:
Cloned trypanosomal calmodulin was expressed in Escherichia coli and purified to homogeneity using hydrophobic interaction chromatography on phenyl-Sepharose. The purified protein was subjected to NMR analysis which allows detailed changes to be observed when, firstly, calcium, and secondly, the drug calmidazolium bind. These spectral changes are the result of conformational changes in the protein and proximity effects due to the drug.