Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Channel Rhodopsins01:11

Channel Rhodopsins

3.4K
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.
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
3.4K
Photoreceptors and Visual Pathways01:22

Photoreceptors and Visual Pathways

10.9K
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,...
10.9K
Anoxygenic Photosynthesis01:30

Anoxygenic Photosynthesis

1.6K
Anoxygenic photosynthesis is a phototrophic process that captures light energy to drive carbon fixation without producing molecular oxygen. Unlike oxygenic photosynthesis, which utilizes water as an electron donor and releases oxygen, anoxygenic phototrophs use alternative electron donors such as hydrogen sulfide (H₂S), elemental sulfur (S⁰), or thiosulfate (S₂O₃²⁻). This process is carried out by diverse groups of bacteria, including purple bacteria, green...
1.6K
The Photochemical Reaction Center01:29

The Photochemical Reaction Center

5.9K
Reaction centers are pigment-protein complexes that initiate energy conversion from photons to chemical entities. Therefore, photochemical reaction center is a more appropriate term that describes these complexes. The Nobel laureates Robert Emerson and William Arnold provided the first experimental evidence of photochemical reaction centers by demonstrating the participation of nearly 2,500 chlorophyll molecules for the release of just one molecule of oxygen. Despite thousands of photosynthetic...
5.9K
Photosystem I01:27

Photosystem I

71.4K
Although structurally similar to photosystem II (PSII), photosystem I (PSI) is has a different electron supplier and electron acceptor.
Both these photosystems work in concert. An excited electron from PSII is relayed to PSI via an electron transport chain in the thylakoid membrane of the chloroplast, which is comprised of the carrier molecule plastoquinone, the dual-protein cytochrome complex, and plastocyanin. As electrons move between PSII and PSI, they lose energy and must be re-energized...
71.4K
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

6.9K
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...
6.9K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

ModBind<sub>dG</sub>: A simulation-based absolute predictor of free energy of binding based on population reweighting.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Coarse-Grained Molecular Dynamics Simulations Reveal Potential Role of Cardiolipin in Lateral Organization of Proteorhodopsin.

Biochemistry·2025
Same author

Structure Characterization of a Disordered Peptide Using In-Droplet Hydrogen/Deuterium Exchange Mass Spectrometry and Molecular Dynamics.

ACS physical chemistry Au·2025
Same author

ModBind, a Rapid Simulation-Based Predictor of Ligand Binding and Off-Rates.

Journal of chemical information and modeling·2024
Same author

Long-Time Scale Simulations Reveal Key Dynamics That Drive the Onset of the N State in the Proteorhodopsin Photocycle.

The journal of physical chemistry. B·2024
Same author

Neutron spin echo shows pHLIP is capable of retarding membrane thickness fluctuations.

Biochimica et biophysica acta. Biomembranes·2024

Related Experiment Video

Updated: Mar 24, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

18.5K

Theoretical Evidence for Multiple Charge Transfer Pathways in Bacteriorhodopsin.

Choongkeun Lee1, Blake Mertz1

  • 1C. Eugene Bennett Department of Chemistry, West Virginia University , Morgantown, West Virginia 26506, United States.

Journal of Chemical Theory and Computation
|March 8, 2016
PubMed
Summary

This study reveals distinct charge transport pathways in bacteriorhodopsin (bR), a membrane protein. Understanding these molecular pathways is key for designing efficient biomolecular electronic devices.

More Related Videos

Atomic Force Microscopy of Red-Light Photoreceptors Using PeakForce Quantitative Nanomechanical Property Mapping
14:13

Atomic Force Microscopy of Red-Light Photoreceptors Using PeakForce Quantitative Nanomechanical Property Mapping

Published on: October 24, 2014

12.2K
Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins
08:39

Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins

Published on: May 22, 2017

18.2K

Related Experiment Videos

Last Updated: Mar 24, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

18.5K
Atomic Force Microscopy of Red-Light Photoreceptors Using PeakForce Quantitative Nanomechanical Property Mapping
14:13

Atomic Force Microscopy of Red-Light Photoreceptors Using PeakForce Quantitative Nanomechanical Property Mapping

Published on: October 24, 2014

12.2K
Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins
08:39

Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins

Published on: May 22, 2017

18.2K

Area of Science:

  • Biophysics
  • Molecular Electronics
  • Protein Science

Background:

  • Biomolecular junctions require understanding molecular structure and conductance.
  • Charge mobility is crucial for electronic device response times.
  • Bacteriorhodopsin (bR) is a well-studied membrane protein.

Purpose of the Study:

  • To theoretically investigate the charge mobility of bacteriorhodopsin (bR).
  • To elucidate the molecular pathways of charge transport in bR.
  • To inform the design of efficient biomolecular-based electronic junctions.

Main Methods:

  • Extended Marcus-Hush theory was employed for theoretical investigation.
  • Charge mobilities for hole and electron transfer were calculated.
  • Analysis of distinct charge hopping pathways within the protein structure.

Main Results:

  • Calculated charge mobilities: 1.3 × 10⁻² cm²/(V s) for holes and 9.7 × 10⁻⁴ cm²/(V s) for electrons.
  • Electron mobility is comparable to experimental values.
  • Hole and electron transfer pathways are distinct, utilizing different transmembrane helices.
  • The electron transfer pathway involves the retinal chromophore.

Conclusions:

  • The tertiary arrangement of proteins directly impacts charge transfer efficiency.
  • Distinct pathways highlight the influence of molecular structure on electronic properties.
  • Provides a template for understanding protein electron transport and designing biomolecular junctions.