Internal motions play an important role in the biological function of proteins and NMR relaxation studies may characterize them over a wide range of frequencies. An experimental pulse scheme is proposed for the measurement of the 13C0-13C ~ cross-relaxation rate. For sensitivity reasons, this measur
Study of protein dynamics in solution by measurement of13Cα-13CO NOE and13CO longitudinal relaxation
✍ Scribed by Lei Zeng; Mark W. F. Fischer; Erik R. P. Zuiderweg
- Publisher
- Springer Netherlands
- Year
- 1996
- Tongue
- English
- Weight
- 464 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0925-2738
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✦ Synopsis
13CC(-13C0 homonuclear NOE and 13CO T~ relaxation were measured for a 20 kDa protein using tripleresonance pulse sequences. The experiments were sufficiently sensitive to obtain statistically significant differences in relaxation parameters over the molecule. The 13C%13C0 cross-relaxation rate, obtained from these data, is directly proportional to an order parameter describing local motion and it is largely independent of the local correlation time. It is therefore a relatively straightforward observable for the identification of local dynamics.
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