Study of visual pigment rhodopsin supramolecular organization in photoreceptor membrane by small angle neutron scattering method with contrast variationтезисы доклада

Дата последнего поиска статьи во внешних источниках: 20 апреля 2016 г.

Работа с тезисами доклада


[1] Study of visual pigment rhodopsin supramolecular organization in photoreceptor membrane by small angle neutron scattering method with contrast variation / T. B. Feldman, A. I. Ivankov, T. N. Murugova et al. // International Conference Condensed Matter Research at IBR-2 reactor. — Dubna, Moscow region, Russia, 2015. — P. 57–58. The visual pigment rhodopsin is a prototypical member of a large G-protein-coupled receptor (GPCR) family, which plays a key role in all regulatory processes of living organisms. Like many other membrane receptors, GPCRs are known to form dimers and high-order oligomers in membranes. However, the supramolecular organization of rhodopsin in photoreceptor membranes is discussed. Atomic force microscopy images of the native rod outer segment disk membranes showing the rows of rhodopsin dimers provide a striking demonstration of their possible supramolecular organization. At the same time there are a number of works, which present the evidence of a rhodopsin monomeric state in the photoreceptor membranes. We have investigated the rhodopsin supramolecular organization in the photoreceptor membranes in the solution by small angle neutron scattering method (SANS). SANS experiments were performed with the various parts of heavy water in the solution (contrast variation method) to obtain the information about the lipid and the protein components separately. It was shown that the packing density of the rhodopsin molecules in the photoreceptor membrane is unusually high. The distance between the centers of the molecules is approximately 56 Å. The probability of the monomeric state of rhodopsin molecules in the photoreceptor membrane, according to our data, is rather high.

Публикация в формате сохранить в файл сохранить в файл сохранить в файл сохранить в файл сохранить в файл сохранить в файл скрыть