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

15.0K
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...
15.0K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

2.0K
2.0K
Protein Folding01:25

Protein Folding

8.8K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.8K
Protein Folding01:22

Protein Folding

112.3K
Overview
112.3K
Protein Folding01:22

Protein Folding

29.7K
29.7K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

14.7K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
14.7K

You might also read

Related Articles

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

Sort by
Same author

Universal negative energetic elasticity in polymer chains: Crossovers among random, self-avoiding, and neighbor-avoiding walks.

Physical review. E·2025
Same author

Phenotype selection due to mutational robustness.

PloS one·2024
Same author

Solvent-Induced Negative Energetic Elasticity in a Lattice Polymer Chain.

Physical review letters·2023
Same author

Evolution enhances mutational robustness and suppresses the emergence of a new phenotype: A new computational approach for studying evolution.

PLoS computational biology·2022
Same author

Emergence of cooperative bistability and robustness of gene regulatory networks.

PLoS computational biology·2020
Same author

The interplay of intrinsic disorder and macromolecular crowding on α-synuclein fibril formation.

The Journal of chemical physics·2016

Related Experiment Video

Updated: May 4, 2026

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis
08:49

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis

Published on: June 20, 2025

1.6K

Structural flexibility of intrinsically disordered proteins induces stepwise target recognition.

Nobu C Shirai1, Macoto Kikuchi1

  • 1Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan.

The Journal of Chemical Physics
|December 17, 2013
PubMed
Summary

Intrinsically disordered proteins (IDPs) use structural flexibility to bind targets with hidden sites through a process called multiform binding, involving intermediate states. This adaptability is a key functional advantage for IDPs.

More Related Videos

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

1.1K
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

2.2K

Related Experiment Videos

Last Updated: May 4, 2026

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis
08:49

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis

Published on: June 20, 2025

1.6K
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

1.1K
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

2.2K

Area of Science:

  • Biophysics
  • Computational Biology
  • Protein Science

Background:

  • Intrinsically disordered proteins (IDPs) lack stable structures but adopt specific conformations upon binding targets.
  • Some IDP-target interactions involve intermediate states, especially when target binding sites are not fully exposed.

Purpose of the Study:

  • To investigate how intrinsically disordered proteins bind to targets with hidden binding sites.
  • To explore the role of intermediate states in IDP-target recognition.

Main Methods:

  • Developed an intrinsically disordered protein (IDP) lattice model based on the HP model.
  • Modeled the IDP as a chain and the target as a coarse-grained object with introduced motion and internal interactions to simulate hidden binding sites.

Main Results:

  • Observed a two-state transition (coupled folding and binding) for targets with unhidden binding sites.
  • Identified an intermediate bound state for targets with hidden binding sites, where the IDP forms various structures.
  • Demonstrated that the intermediate state acts as a scaffold, enabling IDP access to hidden binding sites, a process termed multiform binding.

Conclusions:

  • Structural flexibility of IDPs is crucial for accessing hidden binding sites.
  • Multiform binding via intermediate states is a characteristic and functional advantage of IDPs interacting with complex targets.