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

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

17.5K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
17.5K
Protein Folding01:22

Protein Folding

116.4K
Overview
116.4K

You might also read

Related Articles

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

Sort by
Same author

Cooperativity, dynamics, and the free-energy surfaces of charge-patterned IDPs.

bioRxiv : the preprint server for biology·2026
Same author

Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.

Reports on progress in physics. Physical Society (Great Britain)·2026
Same author

Short autoinhibitory sequences control phase separation of an essential bacterial transcription termination factor.

The EMBO journal·2026
Same author

Time-Resolved Single-Molecule FRET Reveals Length-Dependent Nucleosome Decompaction by Poly(ADP-ribose).

bioRxiv : the preprint server for biology·2026
Same author

Dynamical Buffering of Reconfiguration Dynamics in Intrinsically Disordered Proteins.

JACS Au·2026
Same author

Toward a unified framework for determining conformational ensembles of disordered proteins.

Nature methods·2026

Related Experiment Video

Updated: May 7, 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

3.1K

Identifying Sequence Effects on Chain Dimensions of Disordered Proteins by Integrating Experiments and Simulations.

Andrea Holla1, Erik W Martin2, Thomas Dannenhoffer-Lafage3

  • 1Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.

JACS Au
|December 30, 2024
PubMed
Summary

Intrinsically disordered proteins

More Related Videos

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

1.6K
Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

2.0K

Related Experiment Videos

Last Updated: May 7, 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

3.1K
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

1.6K
Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

2.0K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Biology

Background:

  • Intrinsically disordered proteins (IDPs) lack stable 3D structures.
  • Their conformations are crucial for function and depend on amino acid sequence.
  • Understanding sequence-ensemble relationships is key for IDP research.

Purpose of the Study:

  • To systematically investigate how amino acid composition dictates the conformational ensembles of intrinsically disordered protein regions.
  • To develop a predictive model for disordered protein behavior based on sequence features.

Main Methods:

  • Single-molecule Förster resonance energy transfer (smFRET) spectroscopy.
  • Circular dichroism (CD), nuclear magnetic resonance (NMR), and small-angle X-ray scattering (SAXS).
  • Atomistic simulations with ensemble reweighting and coarse-grained model parametrization.

Main Results:

  • Disordered protein chain dimensions varied up to sixfold based on amino acid composition.
  • Specific residue types (charged, aromatic, polar) significantly influence intrachain interactions.
  • A transferable coarse-grained model accurately described experimental FRET data.

Conclusions:

  • Protein sequence composition is a primary determinant of conformational ensembles in intrinsically disordered regions.
  • Integrating experimental and simulation approaches provides quantitative insights into IDP behavior.
  • The developed model advances the understanding and prediction of disordered protein structures.