A Simple Method to Measure Protein Side-Chain Mobility Using NMR Chemical Shifts
β Scribed by Berjanskii, Mark V.; Wishart, David S.
- Book ID
- 121226255
- Publisher
- American Chemical Society
- Year
- 2013
- Tongue
- English
- Weight
- 720 KB
- Volume
- 135
- Category
- Article
- ISSN
- 0002-7863
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
A simple approach to deriving motional dynamics information of protein and peptide side chains by using 13C NMR relaxation data is presented. By using linear approximation of internal rotational correlation functions, simple equations for relating side-chain conformation, bond rotational amplitudes,
A simple technique for identifying protein secondary structures through the analysis of backbone 13C chemical shifts is described. It is based on the Chemical-Shift Index [Wishart et al. (1992) Biochemistry, 31, 1647-1651] which was originally developed for the analysis of 1H(alpha) chemical shifts.
## Abstract Siteβspecific ^19^F chemical shift and side chain relaxation analysis can be applied on large size proteins. Here, oneβdimensional ^19^F spectra and __T__~1~, __T__~2~ relaxation data were acquired on a SH3 domain in aqueous buffer containing 60% glycerol, and a nineβtransmembrane helic