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

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

2.2K
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...
2.2K
Cryo-electron Microscopy01:28

Cryo-electron Microscopy

3.4K
Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
3.4K

You might also read

Related Articles

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

Sort by
Same author

A bacteriophytochrome Pr/Pfr heterodimer studied through single-particle time-resolved cryo-electron microscopy.

Communications chemistry·2026
Same author

Ultrafast, remote-controlled protonation reaction enables structural changes in a phytochrome.

Science advances·2025
Same author

Observation of early events in the photoactivation of Myxobacterial phytochrome using time-resolved serial femtosecond crystallography.

Communications chemistry·2025
Same author

Structures of myxobacterial phytochrome revealed by cryo-EM using the Spotiton technique and with x-ray crystallography.

Structural dynamics (Melville, N.Y.)·2025
Same author

Exploiting fourth-generation synchrotron radiation for enzyme and photoreceptor characterization.

IUCrJ·2024
Same author

<i>In situ</i> counter-diffusion crystallization and long-term crystal preservation in microfluidic fixed targets for serial crystallography.

Journal of applied crystallography·2024
Same journal

Report of high data rate macromolecular crystallography (HDRMX) meeting, 23 July 2025.

Structural dynamics (Melville, N.Y.)·2026
Same journal

Directional sensitivity of the <math><mrow><mrow><msub><mrow><mi>A</mi></mrow> <mrow><mn>1</mn> <mi>g</mi></mrow></msub></mrow></mrow></math> phonon in biaxially strained bismuth heterofilms studied by transient white light reflectivity.

Structural dynamics (Melville, N.Y.)·2026
Same journal

Erratum: "First experiments with ultrashort, circularly polarized soft x-ray pulses at FLASH2" [Struct. Dyn. <b>12</b>, 034301 (2025)].

Structural dynamics (Melville, N.Y.)·2026
Same journal

<sup>13</sup>C NMR as a foundation for machine learning models of polysaccharides.

Structural dynamics (Melville, N.Y.)·2026
Same journal

Bromodomain dimers: A case study of BRD4 and family-wide AlphaFold predictions.

Structural dynamics (Melville, N.Y.)·2026
Same journal

Integrating metabolomics and histopathology: A method for metabolite recovery from fixed tissue specimens.

Structural dynamics (Melville, N.Y.)·2026
See all related articles

Related Experiment Video

Updated: Aug 8, 2025

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

18.0K

Biological function investigated by time-resolved structure determination.

Marius Schmidt1

  • 1Physics Department, University of Wisconsin-Milwaukee, 3135 North Maryland Avenue, Milwaukee, Wisconsin 53211, USA.

Structural Dynamics (Melville, N.Y.)
|February 27, 2023
PubMed
Summary
This summary is machine-generated.

Researchers are developing advanced imaging techniques to observe life's molecular mechanisms in unprecedented detail. These methods capture rapid biological events across diverse scales, from atomic to cellular levels, and from femtoseconds to hours.

More Related Videos

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.5K
Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.1K

Related Experiment Videos

Last Updated: Aug 8, 2025

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

18.0K
Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.5K
Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.1K

Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Recent advancements in time-resolved X-ray crystallography and cryo-electron microscopy have enabled high-resolution studies of dynamic biological processes.
  • Understanding molecular mechanisms requires observing events across a wide range of spatial and temporal scales.

Purpose of the Study:

  • To review and present methodologies for enhancing the resolution and speed of biological imaging.
  • To illustrate how these advanced techniques provide new insights into the molecular mechanisms of life.

Main Methods:

  • Time-resolved X-ray crystallography
  • Cryo-electron microscopy with time-resolution
  • Development of novel imaging approaches for enhanced speed and resolution.

Main Results:

  • Demonstration of techniques capable of capturing biological events from fractions of Ångströms to micrometers.
  • Observation of responses to chemical and physical stimuli across timescales from femtoseconds to hours.
  • New insights into molecular mechanisms driven by stimuli.

Conclusions:

  • Advanced time-resolved imaging techniques are crucial for understanding dynamic molecular processes.
  • These methods offer unprecedented views into biological responses at various scales.
  • Future research will continue to refine these techniques for deeper biological insights.