Site-specific Labelling with a Metal Chelator for Protein-structure Refinement
A single free Cys sidechain in the N-terminal domain of the E. coli arginine repressor was covalently derivatized with S-cysteaminyl-EDTA for site-specific attachment of paramagnetic metal ions. The effects of chelated metal ions were monitored with 15N-HSQC spectra. Complexation of Co2+, which has a fast relaxing electron spin, resulted in significant pseudocontact shifts, but also in peak doubling which was attributed to the possibility of forming two different stereoisomers of the EDTA-Co2+...[Show more]
|Collections||ANU Research Publications|
|Source:||Journal of Biomolecular NMR|
Items in Open Research are protected by copyright, with all rights reserved, unless otherwise indicated.