Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Negative stain electron microscopy and saturation transfer electron spin resonance spectroscopy have been used to compare the lattice ordering and in-plane membrane mobility of full-length and C-terminally cleaved squid rhodopsin. The C-terminus of squid rhodopsin contains a negatively charged region followed by 9-10 repeats of a proline-rich sequence, not found in rhodopsins other than those of cephalopod invertebrates, but similar proline repeats are found in other, unrelated membrane proteins. We find that the proline repeats cluster the rhodopsins into small groups, interfering with two-dimensional crystallization and maintaining their mobility in the membrane.

Type

Journal article

Journal

FEBS Lett

Publication Date

06/02/1995

Volume

359

Pages

45 - 49

Keywords

Animals, Cell Membrane, Decapodiformes, Electron Spin Resonance Spectroscopy, Hot Temperature, Microscopy, Electron, Peptide Fragments, Photoreceptor Cells, Invertebrate, Proline, Repetitive Sequences, Nucleic Acid, Rhodopsin