✦ LIBER ✦
Quantitative measurement of differential 15NHα/βT2 relaxation rates in a perdeuterated protein by MAS solid-state NMR spectroscopy
✍ Scribed by Veniamin Chevelkov; Anne Diehl; Bernd Reif
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 373 KB
- Volume
- 45
- Category
- Article
- ISSN
- 0749-1581
- DOI
- 10.1002/mrc.2129
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✦ Synopsis
Dynamic parameters become more and more accessible in the study of uniformly isotopically enriched proteins by MAS solid-state NMR. We demonstrate that T 2 -related relaxation properties can quantitatively be determined in a sample of a perdeuterated microcrystalline protein by the measurement of 15 N, 1 H dipole, 15 N CSA cross-correlated relaxation rates. We find that the measured cross-correlated relaxation rates are independent of the MAS rotation frequency, and therefore reflect local dynamic fluctuations of the protein structure.