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

3.1K
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,...
3.1K
IR Spectroscopy: Molecular Vibration Overview01:24

IR Spectroscopy: Molecular Vibration Overview

4.4K
When Infrared (IR) radiation passes through a covalently bonded molecule, the bonds transition from lower to higher vibrational levels. The fundamental vibrational motions that result in infrared absorption can be classified as stretching or bending vibrations.
Stretching vibrations are vibrational motions that occur along the bond line, changing the bond length or distance between two bonded atoms. They are further distinguished as symmetric or asymmetric. In symmetric stretching, the...
4.4K
IR and UV–Vis Spectroscopy of Carboxylic Acids01:28

IR and UV–Vis Spectroscopy of Carboxylic Acids

5.6K
In IR spectroscopy of carboxylic acids, the C=O bond shows a characteristic band between 1710 and 1760 cm⁻¹, and the O–H bond exhibits a broad band between 2500 and 3300 cm⁻¹.
However, the stretching absorptions for the C=O bond vary depending on the structure of carboxylic acids. The C=O bond of the free carboxylic acids shows a higher stretching frequency, 1760 cm−1, while H-bonded carboxylic acids (dimers) exhibit stretching absorptions at a lower frequency,...
5.6K
UV–Vis Spectroscopy: Molecular Electronic Transitions01:16

UV–Vis Spectroscopy: Molecular Electronic Transitions

2.7K
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...
2.7K
IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration01:16

IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration

2.7K
A covalently bonded heteronuclear diatomic molecule can be modeled as two vibrating masses connected by a spring. The vibrational frequency of the bond can be expressed using an equation derived from Hooke's law, which describes how the force applied to stretch or compress a spring is proportional to the displacement of the spring. In this case, the atoms behave like masses, and the bond acts like a spring.
According to Hooke's law, the vibrational frequency is directly proportional to...
2.7K
IR and UV–Vis Spectroscopy of Aldehydes and Ketones01:29

IR and UV–Vis Spectroscopy of Aldehydes and Ketones

7.2K
Infrared spectroscopy, also known as vibrational spectroscopy, is mainly used to determine the types of bonds and functional groups in molecules. In aldehydes and ketones, the carbonyl (C=O) bond shows an absorption around 1710 cm-1. The C=O bond vibration of an aldehyde occurs at lower frequencies than that of a ketone. In addition to the C=O absorption in an aldehyde, the aldehydic C–H bond also gives two peaks in the 2700–2800 cm-1 range. This absorption, coupled with the...
7.2K

You might also read

Related Articles

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

Sort by
Same author

Structural insights into spectral tuning and retinal exchange in cone visual pigments.

Science (New York, N.Y.)·2026
Same author

Deciphering Infrared Difference Spectra of Bovine Rhodopsin in the Amide I Region by Localized Anharmonic Vibrational Calculations.

The journal of physical chemistry. B·2026
Same author

Molecular Properties of a Novel Inward Proton Pump Rhodopsin, GhXeR.

The journal of physical chemistry. B·2026
Same author

Formation of a Proton-Conducting Hydrogen-Bond Network during the L/M Transition of <i>Ns</i>XeR Uncovered by Light-Induced FTIR Spectroscopy.

The journal of physical chemistry letters·2026
Same author

FTIR study of the wild-type and mutant proteins of a viral rhodopsin, OLPVR1.

Biophysics and physicobiology·2026
Same author

Structural and dynamic insights into the biased signaling mechanism of the human kappa opioid receptor.

Nature communications·2025

Related Experiment Video

Updated: Jan 8, 2026

Author Spotlight: Unraveling Vitamin A Transport Mechanisms &#8212; Linking Liver Receptors to Vision Health Through RBPR2 and RBP4 Interactions
08:18

Author Spotlight: Unraveling Vitamin A Transport Mechanisms — Linking Liver Receptors to Vision Health Through RBPR2 and RBP4 Interactions

Published on: October 4, 2024

1.5K

FTIR Spectroscopy of a Viral Rhodopsin, OLPVR2.

Mako Aoyama1, Kota Katayama1,2, Hideki Kandori1,2

  • 1Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.

The Journal of Physical Chemistry. B
|December 23, 2025
PubMed
Summary

Organic Lake Phycodnavirus Rhodopsin 2 (OLPVR2), a viral rhodopsin, functions differently from proton pumps like bacteriorhodopsin. FTIR studies reveal distinct water interactions and chromophore dynamics in OLPVR2, highlighting its unique light-gated ion channel mechanism.

More Related Videos

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

18.3K
A Rhodopsin Transport Assay by High-Content Imaging Analysis
12:11

A Rhodopsin Transport Assay by High-Content Imaging Analysis

Published on: January 16, 2019

6.9K

Related Experiment Videos

Last Updated: Jan 8, 2026

Author Spotlight: Unraveling Vitamin A Transport Mechanisms &#8212; Linking Liver Receptors to Vision Health Through RBPR2 and RBP4 Interactions
08:18

Author Spotlight: Unraveling Vitamin A Transport Mechanisms — Linking Liver Receptors to Vision Health Through RBPR2 and RBP4 Interactions

Published on: October 4, 2024

1.5K
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

18.3K
A Rhodopsin Transport Assay by High-Content Imaging Analysis
12:11

A Rhodopsin Transport Assay by High-Content Imaging Analysis

Published on: January 16, 2019

6.9K

Area of Science:

  • Structural biology
  • Biophysics
  • Microbial biochemistry

Background:

  • Microbial rhodopsins are classified into VR1 and VR2 families, with OLPVR2 belonging to VR2.
  • OLPVR2 is proposed to be a light-gated ion channel, distinct from proton pumps like bacteriorhodopsin (BR).
  • OLPVR2 forms a pentamer with a central ion pathway and possesses a unique water cluster structure.

Purpose of the Study:

  • To investigate the photoexcitation mechanism and structural dynamics of OLPVR2 using low-temperature FTIR spectroscopy.
  • To compare OLPVR2's properties with OLPVR1 and bacteriorhodopsin (BR).
  • To elucidate the role of protein-bound water and counterions in OLPVR2 function.

Main Methods:

  • Low-temperature Fourier Transform Infrared (FTIR) spectroscopy at 77 K and 170 K.
  • Comparative analysis with OLPVR1 and bacteriorhodopsin (BR).
  • Mutation studies to assess counterion effects.

Main Results:

  • Photoexcitation of OLPVR2 induces retinal isomerization and formation of a K intermediate with a distorted chromophore, similar to OLPVR1 and BR.
  • OLPVR2 shows temperature-dependent spectral changes related to protonated carboxylic acids and enhanced chromophore distortion at 170 K.
  • Viral rhodopsins (OLPVR2, OLPVR1) exhibit weaker water hydrogen bonds compared to BR, with a characteristic bridging water molecule interacting equally with counterions.

Conclusions:

  • OLPVR2 functions as a light-gated ion channel with distinct structural and dynamic properties compared to BR.
  • The weaker hydrogen bonding of protein-bound water is a characteristic feature of viral rhodopsins.
  • Specific aspartate residues in OLPVR2 and OLPVR1 play a significant role in counterion interactions.