Amide proton relaxation measurements employing a highly deuterated protein.

@article{Ulmer2004AmidePR,
  title={Amide proton relaxation measurements employing a highly deuterated protein.},
  author={Tobias S Ulmer and Iain D. Campbell and Jonathan T. Boyd},
  journal={Journal of magnetic resonance},
  year={2004},
  volume={166 2},
  pages={
          190-201
        }
}
Proton NMR longitudinal and transverse relaxation rates of unlabelled proteins are generally dominated by the many 1H-1H dipolar interactions so that spin diffusion, rather than molecular or internal motions, governs longitudinal relaxation. Here, relaxation measurements of backbone amide proton (1H(N)) magnetisations have been carried out employing the 99% 2H, 98% 15N labelled, small 2F2 protein domain in 10%/90% H(2)O/D(2)O solution. Under these conditions, the longitudinal relaxation rates… CONTINUE READING
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