## Abstract Site‐specific ^19^F chemical shift and side chain relaxation analysis can be applied on large size proteins. Here, one‐dimensional ^19^F spectra and __T__~1~, __T__~2~ relaxation data were acquired on a SH3 domain in aqueous buffer containing 60% glycerol, and a nine‐transmembrane helic
✦ LIBER ✦
Combining NMR Relaxation with Chemical Shift Perturbation Data to Drive Protein–protein Docking
✍ Scribed by Aalt D. J. van Dijk; Robert Kaptein; Rolf Boelens; Alexandre M. J. J. Bonvin
- Book ID
- 106401315
- Publisher
- Springer Netherlands
- Year
- 2006
- Tongue
- English
- Weight
- 461 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0925-2738
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In this paper we present a method for determining the rotational diffusion tensor from NMR relaxation data using a combination of approximate and exact methods. The approximate method, which is computationally less intensive, computes values of the principal components of the diffusion tensor and es