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Suppression of Diagonal Peaks in TROSY-Type ¹H NMR NOESY Spectra of ¹⁵N-Labeled Proteins

Author： Meissner A. Sørensen O.W.

Publisher： Academic Press

ISSN： 1090-7807

Source： Journal of Magnetic Resonance, Vol.140, Iss.2, 1999-10, pp. : 499-503

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

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Abstract

A novel method for suppression of diagonal peaks in the amide region of NOESY NMR spectra of ¹⁵N-labeled proteins is presented. The method is particularly useful for larger proteins at high magnetic fields where interference between dipolar and chemical shift anisotropy relaxation mechanisms results in large TROSY effects, i.e., large differences in ¹H^N linewidths depending on the spin state of attached ¹⁵N nuclei. In this limit the new TROSY NOESY method does not compromise sensitivity. It is demonstrated using a perdeuterated ¹⁵N-labeled protein sample, Neural Cell Adhesion Molecule 213–308 (NCAM) from rat, in H₂O at 800 MHz.

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