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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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At the molecular level, visual signals trigger transformations in photopigment molecules, resulting in changes in the photoreceptor cell's membrane potential. The photon's energy level is denoted by its wavelength, with each specific wavelength of visible light associated with a distinct color. The spectral range of visible light, classified as electromagnetic radiation, spans from 380 to 720 nm. Electromagnetic radiation wavelengths exceeding 720 nm fall under the infrared category,...
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The eye is a spherical, hollow structure composed of three tissue layers. The outer layer — the fibrous tunic, comprises the sclera — a white structure — and the cornea, which is transparent. The sclera encompasses some of the ocular surface, most of which is not visible. However, the 'white of the eye' is distinctively visible in humans compared to other species. The cornea, a clear covering at the front of the eye, enables light penetration. The eye's middle...
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In Ultraviolet–Visible (UV–Vis) spectroscopy, the absorption of electromagnetic radiation is used to probe the electronic structure of molecules. This technique provides insights into molecular electronic transitions, particularly the movement of electrons between different molecular orbitals. Radiation is absorbed if the energy of the electromagnetic radiation passing through the molecule is precisely equal to the energy difference between the excited and ground states. During this...
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Organic compounds with conjugated double bonds show strong absorption features in the UV–visible region of the electromagnetic spectrum attributed to Ď€ → Ď€* electronic excitations. Generally, a UV–vis absorption spectrum is recorded as a plot of absorbance vs wavelength. The wavelength of maximum absorbance, which manifests as a peak in the absorption spectrum, is denoted as λmax.
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Determination of Photoreceptor Cell Spectral Sensitivity in an Insect Model from In Vivo Intracellular Recordings
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Rhodopsin Absorption from First Principles: Bypassing Common Pitfalls.

Omar Valsson1, Pablo Campomanes2, Ivano Tavernelli2

  • 1MESA+ Institute for Nanotechnology, University of Twente , P.O. Box 217, 7500 AE Enschede, The Netherlands.

Journal of Chemical Theory and Computation
|November 20, 2015
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Summary
This summary is machine-generated.

Understanding bovine rhodopsin’s light absorption requires advanced computational methods. Accurately modeling its protein environment is crucial for predicting vision chromophore spectra and resolving theoretical discrepancies.

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A Rhodopsin Transport Assay by High-Content Imaging Analysis
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Area of Science:

  • Biophysics
  • Computational Chemistry
  • Vision Science

Background:

  • Bovine rhodopsin is a key photosensitive protein for vision.
  • Previous theoretical studies on rhodopsin's chromophore-protein interactions yield conflicting results regarding spectral tuning.

Purpose of the Study:

  • To resolve discrepancies in theoretical models of rhodopsin's spectral properties.
  • To investigate the influence of the protein environment on the retinal chromophore's absorption spectrum.

Main Methods:

  • Utilized extensive quantum mechanical/molecular mechanical (QM/MM) molecular dynamics simulations.
  • Employed a suite of quantum chemical methods: time-dependent density functional theory (TDDFT), CASPT2, NEVPT2, and quantum Monte Carlo (QMC).
  • Analyzed a large number of thermally accessible configurations and a large quantum region (250 atoms) for environmental effects.

Main Results:

  • Accurate prediction of rhodopsin's excitation properties necessitates sampling numerous system configurations.
  • A single, static model can lead to erroneous conclusions, with agreement to experimental data arising from error cancellation.
  • An enhanced protein environment description is vital to correct blue-shifts caused by counterions and account for polarization effects.

Conclusions:

  • The study highlights the importance of dynamic and comprehensive structural sampling for accurate theoretical predictions of rhodopsin's spectral properties.
  • An accurate representation of the protein environment, including polarization and counterion effects, is essential for understanding vision mechanisms.