Purification of cloned trypanosomal calmodulin and preliminary NMR studies.
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.
Sweeney
P J
PJ
Division of Biological Sciences, Hatfield Polytechnic, Hertfordshire, U.K.
Walker
J M
JM
Reid
D G
DG
Elshourbagy
N
N
D000595:Amino Acid Sequence; D000818:Animals; D002118:Calcium / Q000378:metabolism; D002147:Calmodulin / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D002845:Chromatography / Q000379:methods*; D003001:Cloning, Molecular; D004926:Escherichia coli; D007093:Imidazoles / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation; D014345:Trypanosoma / Q000032:analysis* / Q000378:metabolism
D002147:Calmodulin; D007093:Imidazoles; C031938:calmidazolium; D002118:Calcium