Jump to main content
Jump to site search

Issue 11, 2015
Previous Article Next Article

Helical rearrangement of photoactivated rhodopsin in monomeric and dimeric forms probed by high-angle X-ray scattering

Author affiliations

Abstract

Light-induced helical rearrangement of vertebrate visual rhodopsin was directly monitored by high-angle X-ray scattering (HAXS), ranging from Q (= 4π sin θ/λ) = 0.03 Å−1 to Q = 1.5 Å−1. HAXS of nanodiscs containing a single rhodopsin molecule was performed before and after photoactivation of rhodopsin. The intensity difference curve obtained by HAXS agreed with that calculated from the crystal structure of dark state rhodopsin and metarhodopsin II, indicating that the conformational change of monomeric rhodopsin in the membrane is consistent with that occurring in the crystal. On the other hand, the HAXS intensity difference curve of nanodiscs containing two rhodopsin molecules was significantly reduced, similar to that calculated from the crystal structure of the deprotonated intermediate, without a large conformational change. These results suggest that rhodopsin is dimerized in the membrane and that the interaction between rhodopsin molecules modulates structural changes.

Graphical abstract: Helical rearrangement of photoactivated rhodopsin in monomeric and dimeric forms probed by high-angle X-ray scattering

Back to tab navigation

Publication details

The article was received on 25 Apr 2015, accepted on 31 Jul 2015 and first published on 05 Aug 2015


Article type: Paper
DOI: 10.1039/C5PP00175G
Author version
available:
Download author version (PDF)
Photochem. Photobiol. Sci., 2015,14, 1965-1973

  •   Request permissions

    Helical rearrangement of photoactivated rhodopsin in monomeric and dimeric forms probed by high-angle X-ray scattering

    Y. Imamoto, K. Kojima, T. Oka, R. Maeda and Y. Shichida, Photochem. Photobiol. Sci., 2015, 14, 1965
    DOI: 10.1039/C5PP00175G

Search articles by author

Spotlight

Advertisements