Quasi-elastic Neutron Scattering Reveals Ligand-Induced Protein Dynamics of a G-Protein-Coupled Receptor

Utsab R. Shrestha, Suchithranga M.D.C. Perera, Debsindhu Bhowmik, Udeep Chawla, Eugene Mamontov, Michael F. Brown, Xiang Qiang Chu

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


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. 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.

Original languageEnglish (US)
Pages (from-to)4130-4136
Number of pages7
JournalJournal of Physical Chemistry Letters
Issue number20
StatePublished - Oct 20 2016

ASJC Scopus subject areas

  • Materials Science(all)
  • Physical and Theoretical Chemistry


Dive into the research topics of 'Quasi-elastic Neutron Scattering Reveals Ligand-Induced Protein Dynamics of a G-Protein-Coupled Receptor'. Together they form a unique fingerprint.

Cite this