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Quasi-elastic Neutron Scattering Reveals Ligand-Induced Protein Dynamics of a G‑Protein-Coupled Receptor
journal contribution
posted on 2016-09-15, 00:00 authored by Utsab
R. Shrestha, Suchithranga M.
D. C. Perera, Debsindhu Bhowmik, Udeep Chawla, Eugene Mamontov, Michael F. Brown, Xiang-Qiang ChuLight
activation of the visual G-protein-coupled receptor (GPCR)
rhodopsin leads to significant structural fluctuations of the protein
embedded within the membrane yielding the activation of cognate G-protein
(transducin), which initiates biological signaling. Here, we report
a quasi-elastic neutron scattering study of the activation of rhodopsin
as a GPCR prototype. Our results reveal a broadly distributed relaxation
of hydrogen atom dynamics of rhodopsin on a picosecond–nanosecond
time scale, crucial for protein function, as only observed for globular
proteins previously. Interestingly, the results suggest significant
differences in the intrinsic protein dynamics of the dark-state rhodopsin
versus the ligand-free apoprotein, opsin. These differences can be
attributed to the influence of the covalently bound retinal ligand.
Furthermore, an idea of the generic free-energy landscape is used
to explain the GPCR dynamics of ligand-binding and ligand-free protein
conformations, which can be further applied to other GPCR systems.
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Keywords
hydrogen atom dynamicsfree-energy landscapeligand-free protein conformationsquasi-elastic neutronGPCR prototypeprotein functionprotein dynamicsGPCR systemsdark-state rhodopsinligand-free apoproteinactivationGPCR dynamicsglobular proteinsQuasi-elastic Neutron ScatteringLigand-Induced Protein DynamicsG-protein-coupled receptor
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