Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

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...

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

You might also read

Related Articles

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

Sort by

Same author

Test-Time Training Scaling Laws for Chemical Exploration in Drug Design.

Journal of chemical information and modeling·2025

Same author

REINFORCE-ING Chemical Language Models for Drug Discovery.

Journal of chemical information and modeling·2025

Same author

Navigating protein landscapes with a machine-learned transferable coarse-grained model.

Nature chemistry·2025

Same author

QuantumBind-RBFE: Accurate Relative Binding Free Energy Calculations Using Neural Network Potentials.

Journal of chemical information and modeling·2025

Same author

Broadening the Scope of Neural Network Potentials through Direct Inclusion of Additional Molecular Attributes.

Journal of chemical theory and computation·2025

Same author

AMARO: All Heavy-Atom Transferable Neural Network Potentials of Protein Thermodynamics.

Journal of chemical theory and computation·2024

Search research articles

Related Experiment Video

Updated: Dec 12, 2025

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

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

Published on: November 1, 2024

Small Molecule Modulation of Intrinsically Disordered Proteins Using Molecular Dynamics Simulations.

Pablo Herrera-Nieto¹, Adrià Pérez¹, Gianni De Fabritiis^1,2,3

¹Computational Science Laboratory, Universitat Pompeu Fabra, 08003 Barcelona, Spain.

Journal of Chemical Information and Modeling

|August 14, 2020

Summary

Developing drugs for intrinsically disordered proteins is challenging. This study reveals how small molecules like SJ403 bind to the p27 protein, restricting its dynamic behavior.

More Related Videos

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function

Published on: April 26, 2024

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Related Experiment Videos

Last Updated: Dec 12, 2025

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

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

Published on: November 1, 2024

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function

Published on: April 26, 2024

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Area of Science:

Biochemistry
Computational Biology
Drug Discovery

Background:

Intrinsically disordered proteins (IDPs) exhibit dynamic behavior, complicating drug development.
Specific small molecules interacting with IDPs exist, but their binding mechanisms remain unclear.

Purpose of the Study:

To investigate the binding mechanisms of small molecules with intrinsically disordered proteins.
To explore the conformational changes induced by ligand binding in IDPs.

Main Methods:

Utilized extensive molecular dynamics simulations.
Employed adaptive sampling algorithms for free ligand binding studies.
Focused on the D2 sub-domain of the p27 protein and the small molecule SJ403.

Main Results:

Identified multiple protein-ligand bound states.
Characterized loosely oriented interactions with limited contacts between SJ403 and critical p27 residues.
Observed that bound-state conformations are also accessible to the unbound protein.

Conclusions:

Small molecule binding to IDPs like p27 involves restricted conformational space.
The study provides a framework for understanding and designing modulators for IDPs.