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J Biomol NMR. 2003 Mar;25(3):243-8.

Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach.

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  • 1Molecular Structural Biology Unit, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892-4307, USA.


Relaxation compensated constant-time Carr-Purcell-Meiboom-Gill relaxation dispersion experiments for amide protons are presented that detect mus-ms time-scale dynamics of protein backbone amide sites. Because of their ten-fold larger magnetogyric ratio, much shorter 180 degrees pulses can be applied to (1)H than to (15)N spins; therefore, off-resonance effects are reduced and a wider range of effective rf fields can often be used in the case of (1)H experiments. Applications to [(1)H-(15)N]-ubiquitin and [(1)H-(15)N]-perdeuterated HIV-1 protease are discussed. In the case of ubiquitin, we present a pulse sequence that reduces artifacts that arise from homonuclear (3)J(H(N)-H(alpha)) coupling. In the case of the protease, we show that relaxation dispersion of both (1)H and (15)N spins provides a more comprehensive picture of slow backbone dynamics than does the relaxation dispersion of either spin alone. We also compare the relative merits of (1)H versus (15)N transverse relaxation measurements and note the benefits of using a perdeuterated protein to measure the relaxation dispersion of both spin types.

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