Publication Type:Journal Article
Source:Journal of the American Chemical Society, Volume 129, Number 30, pp. 9292-+ (2007)
DOI Name (links to online publication)10.1021/Ja0725201
Keywords:residual dipolar couplings; pseudocontact shifts; nmr structures; macromolecules; complexes; dynamics; chelate; dota; ion
A lanthanide ligand is reported, amenable to be immobilized on a protein surface via cysteine residues. This probe yields large single shifts of the protein nuclei resonances in HSQC NMR spectra and causes significant alignment of the protein in the magnetic field, providing additional structural restraints. Anchoring the probe by two cysteine residues instead of one is highly beneficial for the size of its effects.