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Related Concept Videos

Channel Rhodopsins01:11

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Most organisms use photoreceptors to sense and respond to light. Examples of photoreceptors include bacteriorhodopsins and bacteriophytochromes in some bacteria, phytochromes in plants, and rhodopsins in the photoreceptor cells of the vertebral retina. The light-sensitive property of these receptors is because of the bound chromophores, such as bilin in the phytochromes and retinal in the rhodopsins.
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G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
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GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory...
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G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
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SPECTRAL METHODS FOR STUDY OF THE G-PROTEIN-COUPLED RECEPTOR RHODOPSIN. I. VIBRATIONAL AND ELECTRONIC SPECTROSCOPY.

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Related Experiment Video

Updated: Mar 6, 2026

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors
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CONDENSED-MATTER SPECTROSCOPY SPECTRAL METHODS FOR STUDY OF THE G-PROTEIN-COUPLED RECEPTOR RHODOPSIN. II. MAGNETIC

A V Struts1, A V Barmasov2, M F Brown3

  • 1St. Petersburg State Medical University, 194100 St. Petersburg, Russia; St. Petersburg State University, 199034 St. Petersburg, Russia; University of Arizona, Tucson, AZ 85721 USA.

Optics and Spectroscopy
|March 7, 2017
PubMed
Summary

Spectroscopic studies reveal how G-protein-coupled receptors change shape. Magnetic resonance and optical methods explore receptor structure and dynamics in natural membranes, detailing activation mechanisms.

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G Protein-selective GPCR Conformations Measured Using FRET Sensors in a Live Cell Suspension Fluorometer Assay
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Area of Science:

  • Biophysics
  • Structural Biology
  • Spectroscopy

Background:

  • G-protein-coupled receptors (GPCRs) are crucial membrane proteins involved in cellular signaling.
  • Understanding GPCR structure and dynamics is key to deciphering their function.
  • Previous work reviewed optical spectroscopic methods for GPCRs.

Purpose of the Study:

  • To review magnetic resonance techniques for studying GPCRs.
  • To highlight the advantage of studying GPCRs in their native membrane environment.
  • To elucidate the multi-scale reaction mechanism of GPCR activation.

Main Methods:

  • Electron paramagnetic resonance (EPR) and nuclear magnetic resonance (NMR) spectroscopy.
  • Solid-state 2H and 13C NMR for local structure and dynamics of cofactors.
  • Site-directed spin labeling (SDSL) for larger-scale structural changes.
  • Optical spectroscopy (vibrational, electronic) in conjunction with magnetic resonance.

Main Results:

  • Magnetic resonance methods provide specific structural and dynamical data for GPCRs.
  • GPCRs can be studied within their natural membrane lipid environment.
  • Solid-state NMR reveals local structure and dynamics of bound cofactors and light-induced changes.
  • SDSL monitors structural alterations over larger distances and longer timescales.
  • A multi-scale mechanism explains how cofactor changes initiate large conformational shifts.

Conclusions:

  • Local changes in the retinal cofactor initiate large-scale conformational changes in rhodopsin.
  • GPCR activation involves an ensemble of conformational substates.
  • These substates characterize the dynamically active receptor, providing insights into GPCR signaling.