Site-specific 19 F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid

National Laboratory for Physical Science at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui, People's Republic of China.
Protein Science (Impact Factor: 2.86). 01/2011; 20(1):224-8. DOI: 10.1002/pro.545
Source: PubMed

ABSTRACT Site-specific ¹⁹F chemical shift and side chain relaxation analysis can be applied on large size proteins. Here, one-dimensional ¹⁹F spectra and T₁, T₂ 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.


Available from: Xi Zhaoyong, May 29, 2015
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