Abstract
Paramagnetic effects from lanthanide ions present powerful tools for protein studies by nuclear magnetic resonance (NMR) spectroscopy provided that the lanthanide can be site-specifically and rigidly attached to the protein. A new, particularly small and rigid lanthanide-binding tag, 3-mercapto-2,6-pyridinedicarboxylic acid (3MDPA), was synthesized and attached to two different proteins via a disulfide bond. The complexes of the N-terminal domain of the E. coli arginine repressor (ArgN) with seven different paramagnetic lanthanide ions and Co(2+) were analyzed in detail by NMR spectroscopy. The magnetic susceptibility anisotropy (Delta chi) tensors and metal position were determined from pseudocontact shifts. The 3MDPA tag generated very different Delta chi tensor orientations compared to the previously studied 4-mercaptomethyl-DPA tag, making it a highly complementary and useful tool for protein NMR studies.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
