title: Site-specific ¹⁹F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid.
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.
authors.affiliation: 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.
authors.forename: Pan
authors.initials: P
authors.lastname: Shi
authors.forename: Hu
authors.initials: H
authors.lastname: Wang
authors.forename: Zhaoyong
authors.initials: Z
authors.lastname: Xi
authors.forename: Chaowei
authors.initials: C
authors.lastname: Shi
authors.forename: Ying
authors.initials: Y
authors.lastname: Xiong
authors.forename: Changlin
authors.initials: C
authors.lastname: Tian
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry*; D019852:Diacylglycerol Kinase / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009124:Muscle Proteins; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000737:chemistry; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D018909:src Homology Domains
chemical_list: C557397:4-(trifluoromethyl)phenylalanine; D048868:Adaptor Proteins, Signal Transducing; D009124:Muscle Proteins; C486523:SORBS3 protein, human; D010649:Phenylalanine; D019852:Diacylglycerol Kinase