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Related Concept Videos

Channel Rhodopsins01:11

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 Pathways01:22

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...
X-ray Imaging01:24

X-ray Imaging

German physicist Wilhelm Röntgen (1845–1923) was experimenting with electrical current when he discovered that a mysterious and invisible "ray" would pass through his flesh but leave an outline of his bones on a screen coated with a metal compound. In 1895, Röntgen made the first durable record of the internal parts of a living human: an "X-ray" image (as it came to be called) of his wife’s hand. Scientists worldwide quickly began their own experiments with X-rays, and by 1900, X-ray was widely...
The Photochemical Reaction Center01:29

The Photochemical Reaction Center

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...
Determination of Crystal Structures01:29

Determination of Crystal Structures

In the late 1800s, the revelation that light extended beyond visible wavelengths led to the discovery of X-rays by Wilhelm Roentgen. Recognized as high-energy electromagnetic radiation with short wavelengths, X-rays prompted exploration into their interaction with crystals. Max von Laue proposed in 1912 that the periodic arrangement of atoms, ions, or molecules in crystals would cause them to diffract X-rays, a hypothesis confirmed through experiments with copper sulfate and zinc sulfide...
X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are  scattered by the electron clouds around the sample atoms. The  X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal crystal...

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Related Experiment Video

Updated: Jun 2, 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

X-ray-radiation-induced changes in bacteriorhodopsin structure.

Valentin I Borshchevskiy1, Ekaterina S Round, Alexandr N Popov

  • 1Laboratoire des Protéines Membranaires, Institut de Biologie Structurale J.-P. Ebel, UMR5075 CEA-CNRS-UJF, Grenoble 38027, France.

Journal of Molecular Biology
|May 3, 2011
PubMed
Summary
This summary is machine-generated.

X-ray radiation can alter bacteriorhodopsin (bR) structure, mimicking functional changes. This study reveals X-ray absorption induces protein alterations, potentially misinterpreting bR photointermediate structures.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Photobiology

Background:

  • Bacteriorhodopsin (bR) facilitates light-driven proton transport, crucial for cellular energy transformation.
  • Previous crystallographic studies of bR intermediates show discrepancies, leading to contradictory conclusions on its pumping mechanism.

Purpose of the Study:

  • To quantitatively investigate conformational changes in bacteriorhodopsin induced by X-ray absorption.
  • To assess the impact of X-ray doses on bR structure during crystallographic studies.

Main Methods:

  • High-resolution X-ray crystallography.
  • Quantitative structural analysis.
  • Structural modeling.

Main Results:

  • X-ray doses used in crystallographic studies significantly alter bR structure, particularly in the active site.
  • X-ray absorption triggers retinal isomerization and the loss of water molecule W402 electron density.
  • Observed X-ray-induced changes can mimic authentic functional conformational changes in bR.

Conclusions:

  • X-ray-induced structural modifications in bacteriorhodopsin can lead to misinterpretation of its photointermediate structures.
  • Careful consideration of X-ray radiation effects is necessary for accurate structural studies of bR and similar proteins.