A5102013174- Receptor Mechanisms and Signaling
- Protein Structure and Dynamics
- Mass Spectrometry Techniques and Applications
- Technology Adoption and User Behaviour
- RNA and protein synthesis mechanisms
- Neuropeptides and Animal Physiology
- Neuroendocrine regulation and behavior
- Digital Platforms and Economics
- Lipid Membrane Structure and Behavior
Institute of Biophysics
2019-2020
Chinese Academy of Sciences
2019-2020
Institute of Information Engineering
2019
Cleveland Clinic
2006
Abstract Characterization of the dynamic conformational changes in membrane protein signaling complexes by nuclear magnetic resonance (NMR) spectroscopy remains challenging. Here we report site-specific incorporation 4-trimethylsilyl phenylalanine (TMSiPhe) into proteins, through genetic code expansion. Crystallographic analysis revealed structural that reshaped TMSiPhe-specific amino-acyl tRNA synthetase active site to selectively accommodate trimethylsilyl (TMSi) group. The unique up-field...
Signal transduction by G protein-coupled receptors (GPCRs) is mediated interactions between intracellular proteins and exposed motifs on the cytoplasmic face of these receptors. Arrestins bind to GPCRs modulate receptor function either interfering with heterotrimeric protein signaling or serving as adaptors themselves. Calmodulin interacts triggering a calcium response. We have studied interaction arrestin2 calmodulin elements human V1-vascular vasopressin (hV1R). For this purpose, we...
Abstract While one dimensional 1 H nuclear magnetic resonance (1D H-NMR) spectroscopy is of the most important and convenient method for measuring conformation change in biomacromolecules, characterization protein dynamics large membrane complexes by 1D H-NMR remains challenging, due to difficulty spectra assignment, low signal-to-noise ratio (S/N) need amount protein. Here we report site-specific incorporation 4-trimethylsilyl phenylalanine (TMSiPhe) into proteins, through genetic code...