Abstract
Internal motions in ubiquitin have been studied extensively by NMR. Indeed, ubiquitin has been used for two decades as a standard for biomolecular NMR, and new methods have been frequently validated with experiments on ubiquitin.
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Notes
- 1.
The results of heteronuclear NOE measurements are commonly presented as the ratio of the signal intensities measured at the steady state under effective proton saturation (\(I^{\text {ss}}\)) and at equilibrium (\(I^{\text {eq}}\)). Such ratio is close to 1 for ordered regions and lower for disordered ones, and depends on both \(\sigma _{\text {NH}}\) and R\(_{1}\) [63]:
$$\begin{aligned} \frac{I^{\text {ss}}}{I^{\text {eq}}}=1+\frac{\gamma _{\text {H}}\sigma _{\text {NH}}}{\gamma _{\text {N}}\text {R}_{1}}. \end{aligned}$$In the case of the hexapeptide region \(\sigma _{\text {NH}}\) is smaller than the values measured in the rest of the N-terminal extension, while R\(_{1}\) is larger. Therefore, exploiting the combined effects on \(\sigma _{\text {NH}}\) and R\(_{1}\), \(I^{\text {ss}}/I^{\text {eq}}\) is more sensitive to the presence of order than the two probes individually.
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Salvi, N. (2014). Experimental Results. In: Dynamic Studies Through Control of Relaxation in NMR Spectroscopy. Springer Theses. Springer, Cham. https://doi.org/10.1007/978-3-319-06170-2_5
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