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

Photoreceptors and Visual Pathways01:22

Photoreceptors and Visual Pathways

9.9K
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,...
9.9K
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

2.8K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.8K
Western Blotting01:15

Western Blotting

21.3K
Western blotting is an analytical technique for protein identification. It has various applications in immunology and medicine, including detecting diseases like bovine spongiform encephalopathy, mad cow disease, and human and feline immunodeficiency virus from biological samples.
The technique begins with separating proteins from the sample using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by protein transfer, immunoblotting, and finally, protein detection.
21.3K
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

You might also read

Related Articles

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

Sort by
Same author

Regulatory mechanism of heme-regulated inhibitor through autophosphorylation-driven activation and heme-induced deactivation.

Journal of biochemistry·2026
Same author

Towards the International Conference on Biophysics and Biomedical Sciences: ICBBS 2026.

Biophysics and physicobiology·2026
Same author

Multistep receptor binding of the hepatitis B virus preS1 domain.

Nature communications·2026
Same author

Structural mapping of NTCP distinguishes its dual functionality as a hepatitis B virus receptor and bile acid transporter.

PLoS pathogens·2026
Same author

Crystal and Cryo-EM structure of PPL, a novel hexameric R-type lectin from the poisonous mushroom Pleurocybella porrigens.

Glycobiology·2025
Same author

Structural insights into Influenza A virus RNA polymerase PB1 binding to nuclear import host factor RanBP5.

Biochemical and biophysical research communications·2024
Same journal

Navigating the labyrinth of drugging the disordered.

Biophysical reviews·2026
Same journal

<i>Biophysical Reviews</i>: a forum for publication of review articles from the international biophysics community.

Biophysical reviews·2026
Same journal

Mitochondrial potassium channels: mitochondria-specific mechanism of regulation.

Biophysical reviews·2026
Same journal

Biomolecular condensates in living systems: from function to disease. What to do next.

Biophysical reviews·2026
Same journal

Astrocyte morphology: complex or trivial?

Biophysical reviews·2026
Same journal

Correction to: A quest for greater thermodynamic rigour in the quantitative characterization of protein self-association by direct assessment of sedimentation equilibrium distributions.

Biophysical reviews·2026
See all related articles

Related Experiment Video

Updated: Mar 2, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

1.1K

Seeing the light with BLUF proteins.

Sam-Yong Park1, Jeremy R H Tame2

  • 1Drug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama, 230-0045, Japan.

Biophysical Reviews
|May 17, 2017
PubMed
Summary
This summary is machine-generated.

Blue Light Using Flavin (BLUF) domains are light-activated switches found in many organisms. Recent structural models are clarifying their photo-activation mechanism, potentially enabling new optogenetic tools.

Keywords:
AllosteryFlavinOptogeneticsPhoto-activation

More Related Videos

Bioluminescent Optogenetics 2.0: Harnessing Bioluminescence to Activate Photosensory Proteins In Vitro and In Vivo
07:19

Bioluminescent Optogenetics 2.0: Harnessing Bioluminescence to Activate Photosensory Proteins In Vitro and In Vivo

Published on: August 4, 2021

5.4K
Author Spotlight: Photo Switchable Protein Recruitment for Reversible Patterning in Artificial Cellular Systems
07:10

Author Spotlight: Photo Switchable Protein Recruitment for Reversible Patterning in Artificial Cellular Systems

Published on: February 23, 2024

1.7K

Related Experiment Videos

Last Updated: Mar 2, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

1.1K
Bioluminescent Optogenetics 2.0: Harnessing Bioluminescence to Activate Photosensory Proteins In Vitro and In Vivo
07:19

Bioluminescent Optogenetics 2.0: Harnessing Bioluminescence to Activate Photosensory Proteins In Vitro and In Vivo

Published on: August 4, 2021

5.4K
Author Spotlight: Photo Switchable Protein Recruitment for Reversible Patterning in Artificial Cellular Systems
07:10

Author Spotlight: Photo Switchable Protein Recruitment for Reversible Patterning in Artificial Cellular Systems

Published on: February 23, 2024

1.7K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • BLUF domains are light-sensitive protein modules that regulate biological processes upon blue light exposure.
  • These domains contain a flavin chromophore that absorbs light, initiating downstream signaling events.
  • BLUF proteins are conserved across prokaryotes and eukaryotes, exhibiting diverse structures and functions.

Purpose of the Study:

  • To elucidate the atomic details of BLUF domain photo-activation mechanisms.
  • To resolve conflicting structural and mechanistic models of BLUF domains.
  • To explore the potential of BLUF domains for developing novel optogenetic tools.

Main Methods:

  • X-ray crystallography and Nuclear Magnetic Resonance (NMR) spectroscopy to determine BLUF domain structures.
  • Advanced spectroscopic techniques to analyze early phototransduction events.
  • Computational modeling to investigate photo-activation dynamics.

Main Results:

  • Conflicting structural models have historically hindered a clear understanding of BLUF photo-activation.
  • Advanced spectroscopic and computational studies have yielded diverse conclusions regarding early light-induced events.
  • Emerging structural models are providing improved insights into the detailed photo-activation mechanism.

Conclusions:

  • BLUF domains represent a conserved light-sensing module with a well-preserved structure and mechanism.
  • Ongoing research using advanced techniques is refining our understanding of BLUF domain photo-activation.
  • Improved mechanistic insights may facilitate the design of novel optogenetic applications.