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Spectral methods for study of the G-protein-coupled receptor rhodopsin: I. Vibrational and electronic spectroscopy. / Struts, A.V.; Barmasov, A.V.; Brown, M.F.

In: Optics and Spectroscopy (English translation of Optika i Spektroskopiya), Vol. 118, No. 5, 2015, p. 711-717.

Research output: Contribution to journal › Article

Harvard

Struts, AV, Barmasov, AV & Brown, MF 2015, 'Spectral methods for study of the G-protein-coupled receptor rhodopsin: I. Vibrational and electronic spectroscopy', Optics and Spectroscopy (English translation of Optika i Spektroskopiya), vol. 118, no. 5, pp. 711-717. https://doi.org/10.1134/S0030400X15050240

APA

Struts, A. V., Barmasov, A. V., & Brown, M. F. (2015). Spectral methods for study of the G-protein-coupled receptor rhodopsin: I. Vibrational and electronic spectroscopy. Optics and Spectroscopy (English translation of Optika i Spektroskopiya), 118(5), 711-717. https://doi.org/10.1134/S0030400X15050240

Vancouver

Struts AV, Barmasov AV, Brown MF. Spectral methods for study of the G-protein-coupled receptor rhodopsin: I. Vibrational and electronic spectroscopy. Optics and Spectroscopy (English translation of Optika i Spektroskopiya). 2015;118(5):711-717. https://doi.org/10.1134/S0030400X15050240

Author

Struts, A.V. ; Barmasov, A.V. ; Brown, M.F. / Spectral methods for study of the G-protein-coupled receptor rhodopsin: I. Vibrational and electronic spectroscopy. In: Optics and Spectroscopy (English translation of Optika i Spektroskopiya). 2015 ; Vol. 118, No. 5. pp. 711-717.

BibTeX

@article{f272fe52a83340f88ebe4c85f532e46a,
title = "Spectral methods for study of the G-protein-coupled receptor rhodopsin: I. Vibrational and electronic spectroscopy",
abstract = "http://www.maik.ru/cgi-perl/search.pl?type=abstract&name=optics&number=5&year=15&page=711 Here we review the application of modern spectral methods for the study of G-protein-coupled receptors (GPCRs) using rhodopsin as a prototype. Because X-ray analysis gives us immobile snapshots of protein conformations, it is imperative to apply spectroscopic methods for elucidating their function: vibrational (Raman, FTIR), elec-tronic (UV-visible absorption, fluorescence) spectroscopies, and magnetic resonance (electron paramagnetic resonance, EPR), and nuclear magnetic resonance, NMR). In the first of the two companion articles, we discuss the application of optical spectroscopy for studying rhodopsin in a membrane environment. Information is obtained regarding the time-ordered sequence of events in rhodopsin activation. Isomerization of the chro-mophore and deprotonation of the retinal Schiff base leads to a structural change of the protein involving the motion of helices H5 and H6 in a pH-dependent process. Informa-",
author = "A.V. Struts and A.V. Barmasov and M.F. Brown",
year = "2015",
doi = "10.1134/S0030400X15050240",
language = "English",
volume = "118",
pages = "711--717",
journal = "OPTICS AND SPECTROSCOPY",
issn = "0030-400X",
publisher = "Pleiades Publishing",
number = "5",

}

RIS

TY - JOUR

T1 - Spectral methods for study of the G-protein-coupled receptor rhodopsin: I. Vibrational and electronic spectroscopy

AU - Struts, A.V.

AU - Barmasov, A.V.

AU - Brown, M.F.

PY - 2015

Y1 - 2015

N2 - http://www.maik.ru/cgi-perl/search.pl?type=abstract&name=optics&number=5&year=15&page=711 Here we review the application of modern spectral methods for the study of G-protein-coupled receptors (GPCRs) using rhodopsin as a prototype. Because X-ray analysis gives us immobile snapshots of protein conformations, it is imperative to apply spectroscopic methods for elucidating their function: vibrational (Raman, FTIR), elec-tronic (UV-visible absorption, fluorescence) spectroscopies, and magnetic resonance (electron paramagnetic resonance, EPR), and nuclear magnetic resonance, NMR). In the first of the two companion articles, we discuss the application of optical spectroscopy for studying rhodopsin in a membrane environment. Information is obtained regarding the time-ordered sequence of events in rhodopsin activation. Isomerization of the chro-mophore and deprotonation of the retinal Schiff base leads to a structural change of the protein involving the motion of helices H5 and H6 in a pH-dependent process. Informa-

AB - http://www.maik.ru/cgi-perl/search.pl?type=abstract&name=optics&number=5&year=15&page=711 Here we review the application of modern spectral methods for the study of G-protein-coupled receptors (GPCRs) using rhodopsin as a prototype. Because X-ray analysis gives us immobile snapshots of protein conformations, it is imperative to apply spectroscopic methods for elucidating their function: vibrational (Raman, FTIR), elec-tronic (UV-visible absorption, fluorescence) spectroscopies, and magnetic resonance (electron paramagnetic resonance, EPR), and nuclear magnetic resonance, NMR). In the first of the two companion articles, we discuss the application of optical spectroscopy for studying rhodopsin in a membrane environment. Information is obtained regarding the time-ordered sequence of events in rhodopsin activation. Isomerization of the chro-mophore and deprotonation of the retinal Schiff base leads to a structural change of the protein involving the motion of helices H5 and H6 in a pH-dependent process. Informa-

U2 - 10.1134/S0030400X15050240

DO - 10.1134/S0030400X15050240

M3 - Article

VL - 118

SP - 711

EP - 717

JO - OPTICS AND SPECTROSCOPY

JF - OPTICS AND SPECTROSCOPY

SN - 0030-400X

IS - 5

ER -

ID: 3999769