Small-Angle Neutron Scattering Reveals Energy Landscape for Rhodopsin Photoactivation

Perera, Suchithranga M. D. C.; Chawla, Udeep; Shrestha, Utsab R.; Bhowmik, Debsindhu; Struts, Andrey V.; Qian, Shuo; Chu, Xiang -Qiang; Brown, Michael F.

doi:10.1021/acs.jpclett.8b03048

Small-Angle Neutron Scattering Reveals Energy Landscape for Rhodopsin Photoactivation

Journal Article · Thu Nov 29 00:00:00 EST 2018 · Journal of Physical Chemistry Letters

DOI:https://doi.org/10.1021/acs.jpclett.8b03048· OSTI ID:1492157

Perera, Suchithranga M. D. C. ^[1]; Chawla, Udeep ^[2]; Shrestha, Utsab R. ^[3]; ^[3]; Struts, Andrey V. ^[4]; ^[5]; ^[6]; ^[1]

Univ. of Arizona, Tucson, AZ (United States)
Univ. of Arizona, Tucson, AZ (United States); Univ. of Kentucky, Lexington, KY (United States)
Wayne State Univ., Detroit, MI (United States); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Univ. of Arizona, Tucson, AZ (United States); St. Petersburg State Univ., St. Petersburg (Russia)
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Graduate School of China Academy of Engineering Physics, Beijing (China)

Here, knowledge of the activation principles for G-protein-coupled receptors (GPCRs) is critical to development of new pharmaceuticals. Rhodopsin is the archetype for the largest GPCR family, yet the changes in protein dynamics that trigger signaling are not fully understood. Here we show that rhodopsin can be investigated by small-angle neutron scattering (SANS) in fully protiated detergent micelles under contrast matching to resolve light-induced changes in the protein structure. In SANS studies of membrane proteins, the zwitterionic detergent [(cholamidopropyl)dimethylammonio]-propanesulfonate (CHAPS) is advantageous because of the low contrast difference between the hydrophobic core and hydrophilic head groups as compared with alkyl glycoside detergents. Combining SANS results with quasielastic neutron scattering reveals how changes in volumetric protein shape are coupled (slaved) to the aqueous solvent. Upon light exposure, rhodopsin is swollen by the penetration of water into the protein core, allowing interactions with effector proteins in the visual signaling mechanism.

View Accepted Manuscript (DOE)

Research Organization:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

Sponsoring Organization:: USDOE

Grant/Contract Number:: AC05-00OR22725

OSTI ID:: 1492157

Journal Information:: Journal of Physical Chemistry Letters, Journal Name: Journal of Physical Chemistry Letters Journal Issue: 24 Vol. 9; ISSN 1948-7185

Publisher:: American Chemical SocietyCopyright Statement

Country of Publication:: United States

Language:: English

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Related Subjects

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
GPCR
Rhodopsin
detergent
energy landscape
hydration
membrane proteins
neutron scattering
protein dynamics
slaving
vision

Small-Angle Neutron Scattering Reveals Energy Landscape for Rhodopsin Photoactivation

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