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
Studying the Cytoskeleton01:17

Studying the Cytoskeleton

5.8K
The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
5.8K

You might also read

Related Articles

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

Sort by
Same author

Clinical and Mechanistic Association Between Intestinal Permeability and the Gut Microbiome in Cirrhosis: Role of Phascolarctobacterium.

United European gastroenterology journal·2026
Same author

Presenilin-1 controls glycolysis and identity of pancreatic beta cells.

Communications biology·2026
Same author

A histidine switch controls the pH-responsive self-assembly of a helical protein filament.

bioRxiv : the preprint server for biology·2026
Same author

Cardiovascular effects of metyrapone treatment in patients with mild autonomous cortisol secretion: a secondary analysis.

The Journal of clinical endocrinology and metabolism·2026
Same author

Homocysteine and S-adenosyl-L-homocysteine impair development and methylation in yeast and flies.

Disease models & mechanisms·2026
Same author

MyBioScope: a new frontier in gut microbiome and health research.

Bioresources and bioprocessing·2026

Related Experiment Video

Updated: Jun 7, 2025

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
10:23

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules

Published on: April 25, 2025

204

Methods to Study Structure and Dynamics of FOXO Proteins.

Benjamin Bourgeois1, Tobias Madl2,3

  • 1Medicinal Chemistry, Otto Loewi Research Center, Medical University of Graz, Graz, Austria.

Methods in Molecular Biology (Clifton, N.J.)
|November 20, 2024
PubMed
Summary

We present methods to study the structure and dynamics of FOXO proteins, which are essential transcription factors. Our techniques, using biophysical methods like NMR spectroscopy, can investigate intrinsically disordered regions (IDRs) in FOXOs.

Keywords:
FOXO transcription factorsNMRProtein purificationRelaxation

More Related Videos

Investigating Protein-protein Interactions in Live Cells Using Bioluminescence Resonance Energy Transfer
11:46

Investigating Protein-protein Interactions in Live Cells Using Bioluminescence Resonance Energy Transfer

Published on: May 26, 2014

22.9K
Characterizing Cellular Proteins with In-cell Fast Photochemical Oxidation of Proteins
09:03

Characterizing Cellular Proteins with In-cell Fast Photochemical Oxidation of Proteins

Published on: March 11, 2020

5.5K

Related Experiment Videos

Last Updated: Jun 7, 2025

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
10:23

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules

Published on: April 25, 2025

204
Investigating Protein-protein Interactions in Live Cells Using Bioluminescence Resonance Energy Transfer
11:46

Investigating Protein-protein Interactions in Live Cells Using Bioluminescence Resonance Energy Transfer

Published on: May 26, 2014

22.9K
Characterizing Cellular Proteins with In-cell Fast Photochemical Oxidation of Proteins
09:03

Characterizing Cellular Proteins with In-cell Fast Photochemical Oxidation of Proteins

Published on: March 11, 2020

5.5K

Area of Science:

  • Molecular biology
  • Biophysics
  • Structural biology

Background:

  • Forkhead box proteins (FOXOs) are dynamic transcription factors.
  • They possess intrinsically disordered regions (IDRs) crucial for regulating transcriptional activity.
  • IDRs mediate interactions with cofactors, protein self-interactions, and condensate formation.

Purpose of the Study:

  • To describe generalizable methods for studying FOXO protein structure and dynamics in vitro.
  • To provide a framework for investigating other transcription factors with IDRs.

Main Methods:

  • Utilized a combination of biophysical techniques.
  • Employed nuclear magnetic resonance (NMR) spectroscopy as a key method.
  • Focused on studying intrinsically disordered regions (IDRs) of FOXO proteins.

Main Results:

  • Established methods to analyze the structure and dynamics of FOXO proteins.
  • Demonstrated the utility of biophysical techniques, particularly NMR, for IDR investigation.
  • Provided a blueprint for studying similar IDR-containing transcription factors.

Conclusions:

  • Developed and validated in vitro methods for FOXO structure-dynamic studies.
  • These methods are applicable to understanding the function of IDRs in transcription factors.
  • The described approach serves as a model for future research on intrinsically disordered proteins.