{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Liu Q"],"funding":["National Natural Science Foundation of China"],"pagination":["4857"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7519161"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(1)"],"pubmed_abstract":["Characterization of the dynamic conformational changes in membrane protein signaling complexes by nuclear magnetic resonance (NMR) spectroscopy remains challenging. Here we report the site-specific incorporation of 4-trimethylsilyl phenylalanine (TMSiPhe) into proteins, through genetic code expansion. Crystallographic analysis revealed structural changes that reshaped the TMSiPhe-specific amino-acyl tRNA synthetase active site to selectively accommodate the trimethylsilyl (TMSi) group. The unique up-field <sup>1</sup>H-NMR chemical shift and the highly efficient incorporation of TMSiPhe enabled the characterization of multiple conformational states of a phospho-β2 adrenergic receptor/β-arrestin-1(β-arr1) membrane protein signaling complex, using only 5 μM protein and 20 min of spectrum acc"],"journal":["Nature communications"],"pubmed_title":["DeSiphering receptor core-induced and ligand-dependent conformational changes in arrestin via genetic encoded trimethylsilyl <sup>1</sup>H-NMR probe."],"pmcid":["PMC7519161"],"funding_grant_id":["91640106","31700692","21750003"],"pubmed_authors":["Zhang F","Wang QW","Niu XG","Xiao KH","Jin CW","Lyu X","Zhu ZL","Liu Q","Gong Z","Li ZJ","Wang J","Han MJ","Yang ZY","Sun P","Chen X","Huang SM","Yu X","Wang XY","He QT","Guo SC","Kahsai AW","Song SL","Yang F","Xiao P","Ruan K","Yang Z","Lin JY","Qu CX","Zhu KK","Li FH","Xu Z","Kong W","Sun JP"],"additional_accession":[]},"is_claimable":false,"name":"DeSiphering receptor core-induced and ligand-dependent conformational changes in arrestin via genetic encoded trimethylsilyl <sup>1</sup>H-NMR probe.","description":"Characterization of the dynamic conformational changes in membrane protein signaling complexes by nuclear magnetic resonance (NMR) spectroscopy remains challenging. Here we report the site-specific incorporation of 4-trimethylsilyl phenylalanine (TMSiPhe) into proteins, through genetic code expansion. Crystallographic analysis revealed structural changes that reshaped the TMSiPhe-specific amino-acyl tRNA synthetase active site to selectively accommodate the trimethylsilyl (TMSi) group. The unique up-field <sup>1</sup>H-NMR chemical shift and the highly efficient incorporation of TMSiPhe enabled the characterization of multiple conformational states of a phospho-β2 adrenergic receptor/β-arrestin-1(β-arr1) membrane protein signaling complex, using only 5 μM protein and 20 min of spectrum acc","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Sep","modification":"2026-04-30T05:18:42.55Z","creation":"2020-10-29T09:32:36Z"},"accession":"S-EPMC7519161","cross_references":{"pubmed":["32978402"],"doi":["10.1038/s41467-020-18433-5"]}}