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Strategies for Measurements of Pseudocontact Shifts in Protein NMR Spectroscopy
Author(s) -
John Michael,
Otting Gottfried
Publication year - 2007
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200700510
Subject(s) - spins , paramagnetism , chemistry , diamagnetism , nuclear magnetic resonance spectroscopy , molecule , spectroscopy , biomolecule , nuclear magnetic resonance , chemical shift , chemical physics , solid state nuclear magnetic resonance , crystallography , physics , magnetic field , stereochemistry , condensed matter physics , biochemistry , organic chemistry , quantum mechanics
Paramagnetic metal ions bound to proteins generate a dipolar field that can be accurately probed by pseudocontact shifts (PCS) displayed by the protein’s nuclear spins. PCS are highly useful for determining the coordinates of individual spins in the molecule and for rapid structure determinations of entire protein–protein and protein–ligand complexes. However, PCS measurements require reliable resonance assignments for the molecule in its paramagnetic state and in a diamagnetic reference state. This article discusses different approaches for pairwise resonance assignments, with emphasis on a strategy which exploits chemical exchange between the two states.