Email RIS file
Bookmark
Report an Issue

Quasi-elastic neutron scattering reveals ligand-induced protein dynamics of a G-protein-coupled receptor [electronic resource].

Published
Washington, D.C. : United States. Dept. of Energy, 2016.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy
Physical Description
pages 4,130-4,136 : digital, PDF file
Additional Creators
Oak Ridge National Laboratory, United States. Department of Energy, and United States. Department of Energy. Office of Scientific and Technical Information
Access Online

Availability

I Want It
I Want It

Finding items...

Restrictions on Access
Free-to-read Unrestricted online access
Summary
Light 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. Moreover, 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.
Report Numbers
E 1.99:1329160
Subject(s)
Note
Published through SciTech Connect.
09/15/2016.
Journal of Physical Chemistry Letters 7 ISSN 1948-7185 AM
Utsab R. Shrestha; Suchithranga M. D. C. Perera; Debsindhu Bhowmik; Udeep Chawla; Eugene Mamontov; Michael F. Brown; Xiang -Qiang Chu.
Funding Information
AC05-00OR22725
View MARC record | catkey: 23497801