Fluorescence spectroscopy of rhodopsins: Insights and approaches

Ulrike Alexiev, David Farrens

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

Fluorescence spectroscopy has become an established tool at the interface of biology, chemistry and physics because of its exquisite sensitivity and recent technical advancements. However, rhodopsin proteins present the fluorescence spectroscopist with a unique set of challenges and opportunities due to the presence of the light-sensitive retinal chromophore. This review briefly summarizes some approaches that have successfully met these challenges and the novel insights they have yielded about rhodopsin structure and function. We start with a brief overview of fluorescence fundamentals and experimental methodologies, followed by more specific discussions of technical challenges rhodopsin proteins present to fluorescence studies. Finally, we end by discussing some of the unique insights that have been gained specifically about visual rhodopsin and its interactions with affiliate proteins through the use of fluorescence spectroscopy. This article is part of a Special Issue entitled: Retinal Proteins - You can teach an old dog new tricks.

Original languageEnglish (US)
Pages (from-to)694-709
Number of pages16
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1837
Issue number5
DOIs
StatePublished - 2014

Fingerprint

Rhodopsin
Fluorescence Spectrometry
Fluorescence spectroscopy
Fluorescence
Proteins
Physics
Chromophores
Dogs
Light

Keywords

  • Fluorescence spectroscopy
  • Retinal protein
  • Site-directed fluorescence labeling
  • Visual rhodopsin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology

Cite this

Fluorescence spectroscopy of rhodopsins : Insights and approaches. / Alexiev, Ulrike; Farrens, David.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1837, No. 5, 2014, p. 694-709.

Research output: Contribution to journalArticle

@article{80860935f0cf4586b24eb41e55ba343c,
title = "Fluorescence spectroscopy of rhodopsins: Insights and approaches",
abstract = "Fluorescence spectroscopy has become an established tool at the interface of biology, chemistry and physics because of its exquisite sensitivity and recent technical advancements. However, rhodopsin proteins present the fluorescence spectroscopist with a unique set of challenges and opportunities due to the presence of the light-sensitive retinal chromophore. This review briefly summarizes some approaches that have successfully met these challenges and the novel insights they have yielded about rhodopsin structure and function. We start with a brief overview of fluorescence fundamentals and experimental methodologies, followed by more specific discussions of technical challenges rhodopsin proteins present to fluorescence studies. Finally, we end by discussing some of the unique insights that have been gained specifically about visual rhodopsin and its interactions with affiliate proteins through the use of fluorescence spectroscopy. This article is part of a Special Issue entitled: Retinal Proteins - You can teach an old dog new tricks.",
keywords = "Fluorescence spectroscopy, Retinal protein, Site-directed fluorescence labeling, Visual rhodopsin",
author = "Ulrike Alexiev and David Farrens",
year = "2014",
doi = "10.1016/j.bbabio.2013.10.008",
language = "English (US)",
volume = "1837",
pages = "694--709",
journal = "Biochimica et Biophysica Acta - Bioenergetics",
issn = "0005-2728",
publisher = "Elsevier",
number = "5",

}

TY - JOUR

T1 - Fluorescence spectroscopy of rhodopsins

T2 - Biochimica et Biophysica Acta - Bioenergetics

AU - Alexiev, Ulrike

AU - Farrens, David

PY - 2014

Y1 - 2014

N2 - Fluorescence spectroscopy has become an established tool at the interface of biology, chemistry and physics because of its exquisite sensitivity and recent technical advancements. However, rhodopsin proteins present the fluorescence spectroscopist with a unique set of challenges and opportunities due to the presence of the light-sensitive retinal chromophore. This review briefly summarizes some approaches that have successfully met these challenges and the novel insights they have yielded about rhodopsin structure and function. We start with a brief overview of fluorescence fundamentals and experimental methodologies, followed by more specific discussions of technical challenges rhodopsin proteins present to fluorescence studies. Finally, we end by discussing some of the unique insights that have been gained specifically about visual rhodopsin and its interactions with affiliate proteins through the use of fluorescence spectroscopy. This article is part of a Special Issue entitled: Retinal Proteins - You can teach an old dog new tricks.

AB - Fluorescence spectroscopy has become an established tool at the interface of biology, chemistry and physics because of its exquisite sensitivity and recent technical advancements. However, rhodopsin proteins present the fluorescence spectroscopist with a unique set of challenges and opportunities due to the presence of the light-sensitive retinal chromophore. This review briefly summarizes some approaches that have successfully met these challenges and the novel insights they have yielded about rhodopsin structure and function. We start with a brief overview of fluorescence fundamentals and experimental methodologies, followed by more specific discussions of technical challenges rhodopsin proteins present to fluorescence studies. Finally, we end by discussing some of the unique insights that have been gained specifically about visual rhodopsin and its interactions with affiliate proteins through the use of fluorescence spectroscopy. This article is part of a Special Issue entitled: Retinal Proteins - You can teach an old dog new tricks.

KW - Fluorescence spectroscopy

KW - Retinal protein

KW - Site-directed fluorescence labeling

KW - Visual rhodopsin

UR - http://www.scopus.com/inward/record.url?scp=84897116696&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84897116696&partnerID=8YFLogxK

U2 - 10.1016/j.bbabio.2013.10.008

DO - 10.1016/j.bbabio.2013.10.008

M3 - Article

VL - 1837

SP - 694

EP - 709

JO - Biochimica et Biophysica Acta - Bioenergetics

JF - Biochimica et Biophysica Acta - Bioenergetics

SN - 0005-2728

IS - 5

ER -