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Strategies for Measurements of Pseudocontact Shifts in Protein NMR Spectroscopy

✍ Scribed by Michael John; Gottfried Otting

Publisher
John Wiley and Sons
Year
2007
Tongue
English
Weight
641 KB
Volume
8
Category
Article
ISSN
1439-4235

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✦ Synopsis

Abstract

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.

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