Abstract
Frog rod outer segment (ROS) disc membranes are investigated by three-dimensional electron microscopy of aperiodic structures. Out of the various chemical constituents of these membranes only the visual pigment rhodopsin is examined. It is suggested that rhodopsin molecules are dumb-bell shaped and it is shown that in small areas they are not statistically arranged. Most rhodopsin molecules are tilted 26±2° away from the position normal to the membrane thus showing angles α<90° or α>90°. Within the small part of the disc membrane investigated the long rhodopsin axes lie in planes parallel to the xy-plane, the y-axis being parallel with the connecting cilium of ROS. In the membrane cut-outs reconstructed there are aggregates of five to nine rhodopsin molecules either with α>90° or α<90° only. In adjacent disc membranes all the bigger aggregates appear at the same site and with the same magnitude of α.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.