Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Channel Rhodopsins

Channel Rhodopsins

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,...

Photoreceptors and Visual Pathways

Photoreceptors and Visual Pathways

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, whereas...

You might also read

Related Articles

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

Sort by

Same author

High-resolution structure of monomorphic Aβ<sub>1-40</sub> fibrils.

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

Same author

Through-space donor-acceptor homoconjugation strategies for emissive radical species.

Chemical science·2026

Same author

Aducanumab binding to Aβ<sub>1-42</sub> fibrils alters dynamics of the N-terminal tail while preserving the fibril core.

Proceedings of the National Academy of Sciences of the United States of America·2025

Same author

Atomic Structure of GNNQQNY Nanocrystals: A Validated Approach for Polymorphic Amyloids.

The journal of physical chemistry letters·2025

Same author

Aducanumab Binding to Aβ<sub>1-42</sub> Fibrils Alters Dynamics of the N-Terminal Tail While Preserving the Fibril Core.

bioRxiv : the preprint server for biology·2025

Same author

The Role of Macromolecular Crowding in Cytoskeletal Organization.

Sub-cellular biochemistry·2025

Search research articles

Related Experiment Video

Updated: Jun 19, 2026

Electrophysiological Methods for Measuring Photopigment Levels in Drosophila Photoreceptors

Electrophysiological Methods for Measuring Photopigment Levels in Drosophila Photoreceptors

Published on: June 2, 2022

DNP enhanced frequency-selective TEDOR experiments in bacteriorhodopsin.

Vikram S Bajaj¹, Melody L Mak-Jurkauskas, Marina Belenky

¹Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)

|October 27, 2009

Summary

We introduce frequency-selective (FS) Transverse-Electric Dipole Oscillation Resonance (TEDOR) for precise carbon-13 and nitrogen-15 distance measurements in solid samples. This method enhances structural analysis of biomolecules like bacteriorhodopsin.

More Related Videos

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

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

Published on: June 27, 2014

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

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

Published on: May 22, 2017

Related Experiment Videos

Last Updated: Jun 19, 2026

Electrophysiological Methods for Measuring Photopigment Levels in Drosophila Photoreceptors

Electrophysiological Methods for Measuring Photopigment Levels in Drosophila Photoreceptors

Published on: June 2, 2022

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

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

Published on: June 27, 2014

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

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

Published on: May 22, 2017

Area of Science:

Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy
Structural biology
Biophysics

Background:

Accurate internuclear distance measurements are crucial for determining the structure of biomolecules.
Existing methods like REDOR and other TEDOR variants have limitations in quantitative analysis and spectral assignment.
Uniformly labeled samples (U-\[(13)C,(15)N]) are essential for detailed structural studies.

Purpose of the Study:

To present a novel frequency-selective (FS) TEDOR technique for multiple (13)C-(15)N distance measurements in uniformly labeled solids.
To validate the FS-TEDOR sequence for quantitative spectral assignments and distance measurements.
To integrate dynamic nuclear polarization (DNP) with FS-TEDOR for enhanced sensitivity and spectral resolution.

Main Methods:

Development and application of the frequency-selective (FS) TEDOR pulse sequence.
Measurement of (13)C-(15)N distances in U-\[(13)C,(15)N]-asparagine.
Integration of high-frequency dynamic nuclear polarization (DNP) into the FS-TEDOR protocol.
Acquisition of a resolved correlation spectrum of the Arg-(13)C(gamma)-(15)N(epsilon) region in U-\[(13)C,(15)N]-bacteriorhodopsin.

Main Results:

FS-TEDOR successfully measured (13)C-(15)N distances in asparagine, showing good agreement with established methods.
The integration of DNP with FS-TEDOR allowed for the recording of a resolved correlation spectrum in bacteriorhodopsin.
Six out of seven expected cross-peaks in the Arg-(13)C(gamma)-(15)N(epsilon) region of bacteriorhodopsin were resolved, aligning with its primary sequence.

Conclusions:

FS-TEDOR is a powerful new approach for quantitative (13)C-(15)N distance measurements in uniformly labeled solid samples.
The combination of FS-TEDOR and DNP significantly enhances spectral resolution and sensitivity for studying complex biomolecules.
This technique provides valuable insights into the structure of membrane proteins like bacteriorhodopsin.