✦ LIBER ✦
Site-specific 19F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid
✍ Scribed by Pan Shi; Hu Wang; Zhaoyong Xi; Chaowei Shi; Ying Xiong; Changlin Tian
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 2010
- Tongue
- English
- Weight
- 373 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0961-8368
- DOI
- 10.1002/pro.545
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✦ Synopsis
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 helices membrane protein diacyl‐glycerol kinase (DAGK) in dodecyl phosphochoine (DPC) micelles. The high quality of the data indicates that this method can be applied to site‐specifically analyze side chain internal mobility of membrane proteins or large size proteins.