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

2.1K
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...
2.1K
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

4.3K
Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
4.3K

You might also read

Related Articles

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

Sort by
Same author

Structural and mutational insights define ERMA as the ER Mg<sup>2+</sup> ATPase and reservoir gatekeeper.

Science advances·2026
Same author

Snapshots of the dynamic basis of NTSR1 G protein subtype promiscuity.

Nature·2026
Same author

Purification of post-transcriptionally modified tRNAs for enhanced cell-free translation systems.

Nucleic acids research·2026
Same author

Non-equilibrium snapshots of ligand efficacy at the μ-opioid receptor.

Nature·2025
Same author

Parallel stopped-flow interrogation of diverse biological systems at the single-molecule scale.

Nature methods·2025
Same author

Metabolic Flexibility of Microglia: Energy Substrate Utilization and Impact on Neuronal Metabolism.

Journal of neurochemistry·2025

Related Experiment Video

Updated: Jun 21, 2025

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
06:48

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

3.5K

Single-Molecule Imaging of Integral Membrane Protein Dynamics and Function.

Arnab Modak1, Zeliha Kilic1, Kanokporn Chattrakun1

  • 1Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA; email: arnab.modak@stjude.org, zeliha.kilic@stjude.org, kanokporn.chattrakun@stjude.org, daniel.terry@stjude.org, ravi.kalathur@stjude.org, scott.blanchard@stjude.org.

Annual Review of Biophysics
|July 16, 2024
PubMed
Summary

Single-molecule FRET (smFRET) advances the study of integral membrane proteins (IMPs), revealing transient states critical for cellular function and drug development. This method aids in understanding IMP structure and mechanism of action.

Keywords:
fluorescence resonance energy transfergenetic code expansionintegral membrane proteinsintrinsically dynamic systemsmetastable energy landscapesingle-molecule imaging

More Related Videos

Single-Molecule Imaging of Lateral Mobility and Ion Channel Activity in Lipid Bilayers using Total Internal Reflection Fluorescence TIRF Microscopy
08:55

Single-Molecule Imaging of Lateral Mobility and Ion Channel Activity in Lipid Bilayers using Total Internal Reflection Fluorescence TIRF Microscopy

Published on: February 17, 2023

3.1K
High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy
15:13

High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy

Published on: July 25, 2014

11.4K

Related Experiment Videos

Last Updated: Jun 21, 2025

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
06:48

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

3.5K
Single-Molecule Imaging of Lateral Mobility and Ion Channel Activity in Lipid Bilayers using Total Internal Reflection Fluorescence TIRF Microscopy
08:55

Single-Molecule Imaging of Lateral Mobility and Ion Channel Activity in Lipid Bilayers using Total Internal Reflection Fluorescence TIRF Microscopy

Published on: February 17, 2023

3.1K
High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy
15:13

High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy

Published on: July 25, 2014

11.4K

Area of Science:

  • Biochemistry and biophysics
  • Molecular biology
  • Structural biology

Background:

  • Integral membrane proteins (IMPs) are crucial for cellular functions and are major drug targets.
  • Investigating IMPs' structure-function relationships is essential for understanding cellular processes and developing therapeutics.
  • Traditional methods face challenges in capturing the dynamic nature of IMPs.

Purpose of the Study:

  • To review the practical foundations for using single-molecule Förster Resonance Energy Transfer (smFRET) to study polytopic IMPs.
  • To provide an overview of the technical and conceptual frameworks for smFRET applications in IMP research.
  • To highlight smFRET's utility in understanding IMP conformational dynamics and guiding drug discovery.

Main Methods:

  • Focus on single-molecule Förster Resonance Energy Transfer (smFRET) techniques.
  • Application of smFRET for examining polytopic integral membrane proteins.
  • Utilizing smFRET data for structural and drug mechanism-of-action investigations.

Main Results:

  • smFRET methods reveal transient conformational states critical to IMP function.
  • smFRET data can guide structural investigations of IMPs.
  • smFRET aids in understanding drug mechanisms of action at the molecular level.

Conclusions:

  • Single-molecule FRET is a powerful tool for studying integral membrane protein dynamics.
  • This technique provides insights into transient conformational states essential for IMP function.
  • Future advancements in smFRET will be paramount for progress in IMP research and drug development.