KFU. Card publication. Small-angle neutron and X-ray scattering analysis of the supramolecular organization of rhodopsin in photoreceptor membrane

- RUS
- 中文
- ES

SMALL-ANGLE NEUTRON AND X-RAY SCATTERING ANALYSIS OF THE SUPRAMOLECULAR ORGANIZATION OF RHODOPSIN IN PHOTORECEPTOR MEMBRANE

Form of presentation

Articles in international journals and collections

Year of publication

2019

��

��

Authors, employees of KFU

Belushkin Aleksandr Vladislavovich, author

Other authors

Feldman Tatiana , author

Gordeliy Valentin , author

Ivankov Oleksandr , author

Kolchugina Irina , author

Kuklin Alexander , author

Murugova Tatiana , author

Ostrovsky Mikhail , author

Round Adam , author

Smitienko Olga , author

Yakovleva Marina , author

Bibliographic description in the original language

Tatiana B. Feldman Small-angle neutron and X-ray scattering analysis of the supramolecular organization of rhodopsin in photoreceptor membrane /Tatiana B. Feldmana, Oleksandr I. Ivankovc, Alexander I. Kuklin, Tatiana N. Murugova, Marina A. Yakovleva, Olga A. Smitienko, Irina B. Kolchugina, Adam Round, Valentin I. Gordeliy, Alexander V. Belushkin, Mikhail A. Ostrovsky // Biochimica et Biophysica Acta (BBA) - Biomembranes. - 2019. - 1861. - 183000-183006.

Annotation

The supramolecular organization of the visual pigment rhodopsin in the photoreceptor membrane remains contentious. Specifically, whether this G protein-coupled receptor functions as a monomer or dimer remains unknown, as does the presence or absence of ordered packing of rhodopsin molecules in the photoreceptor membrane. Completely opposite opinions have been expressed on both issues. Herein, using small-angle neutron and X-ray scattering approaches, we performed a comparative analysis of the structural characteristics of the photoreceptor membrane samples in buffer, both in the outer segment of photoreceptor cells, and in the free photoreceptor disks. The average distance between the centers of two neighboring rhodopsin molecules was found to be ~5.8 nm in both cases. The results indicate an unusually high packing density of rhodopsin molecules in the photoreceptor membrane, but molecules appear to be randomly distributed in the membrane without any regular ordering.

Keywords

Rhodopsin, Photoreceptor membrane, Oligomerization, Supramolecular organization, SANS, SAXS

The name of the journal

Biochimica et Biophysica Acta - Biomembranes

URL

https://www.sciencedirect.com/science/article/pii/S0005273619301191?dgcid=coauthor

Please use this ID to quote from or refer to the card

https://repository.kpfu.ru/eng/?p_id=206809&p_lang=2

Full metadata record

Field DC	Value	Language
dc.contributor.author	Belushkin Aleksandr Vladislavovich	ru_RU
dc.contributor.author	Feldman Tatiana	ru_RU
dc.contributor.author	Gordeliy Valentin	ru_RU
dc.contributor.author	Ivankov Oleksandr	ru_RU
dc.contributor.author	Kolchugina Irina	ru_RU
dc.contributor.author	Kuklin Alexander	ru_RU
dc.contributor.author	Murugova Tatiana	ru_RU
dc.contributor.author	Ostrovsky Mikhail	ru_RU
dc.contributor.author	Round Adam	ru_RU
dc.contributor.author	Smitienko Olga	ru_RU
dc.contributor.author	Yakovleva Marina	ru_RU
dc.date.accessioned	2019-01-01T00:00:00Z	ru_RU
dc.date.available	2019-01-01T00:00:00Z	ru_RU
dc.date.issued	2019	ru_RU
dc.identifier.citation	Tatiana B. Feldman Small-angle neutron and X-ray scattering analysis of the supramolecular organization of rhodopsin in photoreceptor membrane /Tatiana B. Feldmana, Oleksandr I. Ivankovc, Alexander I. Kuklin, Tatiana N. Murugova, Marina A. Yakovleva, Olga A. Smitienko, Irina B. Kolchugina, Adam Round, Valentin I. Gordeliy, Alexander V. Belushkin, Mikhail A. Ostrovsky // Biochimica et Biophysica Acta (BBA) - Biomembranes. - 2019. - 1861. - 183000-183006.	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/eng/?p_id=206809&p_lang=2	ru_RU
dc.description.abstract	Biochimica et Biophysica Acta - Biomembranes	ru_RU
dc.description.abstract	The supramolecular organization of the visual pigment rhodopsin in the photoreceptor membrane remains contentious. Specifically, whether this G protein-coupled receptor functions as a monomer or dimer remains unknown, as does the presence or absence of ordered packing of rhodopsin molecules in the photoreceptor membrane. Completely opposite opinions have been expressed on both issues. Herein, using small-angle neutron and X-ray scattering approaches, we performed a comparative analysis of the structural characteristics of the photoreceptor membrane samples in buffer, both in the outer segment of photoreceptor cells, and in the free photoreceptor disks. The average distance between the centers of two neighboring rhodopsin molecules was found to be ~5.8 nm in both cases. The results indicate an unusually high packing density of rhodopsin molecules in the photoreceptor membrane, but molecules appear to be randomly distributed in the membrane without any regular ordering.	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	Rhodopsin	ru_RU
dc.subject	Photoreceptor membrane	ru_RU
dc.subject	Oligomerization	ru_RU
dc.subject	Supramolecular organization	ru_RU
dc.subject	SANS	ru_RU
dc.subject	SAXS	ru_RU
dc.title	Small-angle neutron and X-ray scattering analysis of the supramolecular organization of rhodopsin in photoreceptor membrane	ru_RU
dc.type	Articles in international journals and collections	ru_RU