Application of Spectral Methods for the Study of Rhodopsin – G-Protein-Coupled receptor. II Magnetic resonance methods

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Application of Spectral Methods for the Study of Rhodopsin – G-Protein-Coupled receptor. II Magnetic resonance methods. / Struts, A.V.; Barmasov, A.V.; Brown, M.F.

In: Optics and Spectroscopy (English translation of Optika i Spektroskopiya), Vol. 120, No. 2, 2016, p. 286-293.

Research output: Contribution to journal › Article › peer-review

BibTeX

@article{b6dcbcdfab39485eb98c5e6bc85ce211,

title = "Application of Spectral Methods for the Study of Rhodopsin – G-Protein-Coupled receptor. II Magnetic resonance methods",

abstract = "The recent achievements are reviewed in the studies of G-protein-coupled receptors with the help of magnetic resonance methods including the works performed by the authors. In the same way as optical methods discussed in the previous part, electron spin resonance (EPR) and nuclear magnetic resonance (NMR) provide more, and, importantly, independent structural data on protein, and, in addition, information on the kinetics of conformational transitions and molecular mobility of the protein. An additional advantage is the opportunity to explore the natural membrane receptors in the environment.",

keywords = "мембраны, родопсин, рецепторы, сопряжённые с G-белком, сигнальная трансдукция, ЭПР, ЯМР",

author = "A.V. Struts and A.V. Barmasov and M.F. Brown",

year = "2016",

doi = "10.1134/S0030400X16010197",

language = "English",

volume = "120",

pages = "286--293",

journal = "OPTICS AND SPECTROSCOPY",

issn = "0030-400X",

publisher = "Pleiades Publishing",

number = "2",

}

RIS

TY - JOUR

T1 - Application of Spectral Methods for the Study of Rhodopsin – G-Protein-Coupled receptor. II Magnetic resonance methods

AU - Struts, A.V.

AU - Barmasov, A.V.

AU - Brown, M.F.

PY - 2016

Y1 - 2016

N2 - The recent achievements are reviewed in the studies of G-protein-coupled receptors with the help of magnetic resonance methods including the works performed by the authors. In the same way as optical methods discussed in the previous part, electron spin resonance (EPR) and nuclear magnetic resonance (NMR) provide more, and, importantly, independent structural data on protein, and, in addition, information on the kinetics of conformational transitions and molecular mobility of the protein. An additional advantage is the opportunity to explore the natural membrane receptors in the environment.

AB - The recent achievements are reviewed in the studies of G-protein-coupled receptors with the help of magnetic resonance methods including the works performed by the authors. In the same way as optical methods discussed in the previous part, electron spin resonance (EPR) and nuclear magnetic resonance (NMR) provide more, and, importantly, independent structural data on protein, and, in addition, information on the kinetics of conformational transitions and molecular mobility of the protein. An additional advantage is the opportunity to explore the natural membrane receptors in the environment.

KW - мембраны

KW - родопсин

KW - рецепторы

KW - сопряжённые с G-белком

KW - сигнальная трансдукция

KW - ЭПР

KW - ЯМР

UR - https://www.elibrary.ru/item.asp?doi=10.7868/S0030403416010207

U2 - 10.1134/S0030400X16010197

DO - 10.1134/S0030400X16010197

M3 - Article

VL - 120

SP - 286

EP - 293

JO - OPTICS AND SPECTROSCOPY

JF - OPTICS AND SPECTROSCOPY

SN - 0030-400X

IS - 2

ER -

ID: 7546830