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

18.0K
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...
18.0K
Protein Folding01:25

Protein Folding

8.4K
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...
8.4K
Protein Organization01:13

Protein Organization

140.4K
Overview
140.4K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.2K
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...
18.2K
Protein and Protein Structure02:15

Protein and Protein Structure

80.5K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
80.5K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

11.2K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
11.2K

You might also read

Related Articles

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

Sort by
Same author

Complex Effects of Salt on Small-Angle X-ray Scattering of BSA Originate from the Interplay of Ions and Hydration Water.

The journal of physical chemistry letters·2026
Same author

Counteraction of HMGB1 at ss-dsDNA junctions maintains liquidity of protamine-DNA co-condensates.

bioRxiv : the preprint server for biology·2026
Same author

A membrane insertion code for intrinsically disordered proteins.

bioRxiv : the preprint server for biology·2026
Same author

Measuring bridging forces in protein-DNA condensates.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

DIRseq as a method for predicting drug-interacting residues of intrinsically disordered proteins from sequences.

eLife·2025
Same author

Correlated Segments of Intrinsically Disordered Proteins as Drivers of Homotypic Phase Separation.

JACS Au·2025

Related Experiment Video

Updated: Aug 29, 2025

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

2.1K

Sequence-Dependent Backbone Dynamics of Intrinsically Disordered Proteins.

Souvik Dey1, Matthew MacAinsh1, Huan-Xiang Zhou1,2

  • 1Department of Chemistry, University of Illinois at Chicago, Chicago, Illinois 60607, United States.

Journal of Chemical Theory and Computation
|September 9, 2022
PubMed
Summary
This summary is machine-generated.

Intrinsically disordered proteins (IDPs) use sequence to control function via backbone dynamics. Local and long-range interactions, along with glycines, dictate protein flexibility, enabling adaptable responses to binding partners.

More Related Videos

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

2.2K
Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

15.5K

Related Experiment Videos

Last Updated: Aug 29, 2025

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

2.1K
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

2.2K
Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

15.5K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Biology

Background:

  • Intrinsically disordered proteins (IDPs) lack stable 3D structures, posing challenges in understanding sequence-function relationships.
  • Protein dynamics are increasingly recognized as critical mediators of IDP function, analogous to structure in folded proteins.

Purpose of the Study:

  • To establish general principles linking amino acid sequence to backbone dynamics in IDPs.
  • To investigate how sequence dictates flexibility and motion across different timescales.

Main Methods:

  • Conducted extensive molecular dynamics (MD) simulations for eight distinct IDPs.
  • Analyzed residue-level dynamics, local interactions, secondary structure propensity, and long-range contacts.

Main Results:

  • Identified specific sequence motifs and residue types (e.g., glycine) that govern protein dynamics.
  • Observed that local interactions and secondary structures rigidify specific residue blocks.
  • Demonstrated that long-range contacts and secondary structure packing influence dynamics across larger protein regions.
  • Showed that glycines promote fast dynamics and mediate diverse interaction modes.

Conclusions:

  • Protein backbone dynamics in IDPs are directly encoded by their amino acid sequence.
  • Sequence-determined dynamics allow IDPs to exhibit varied responses to binding partners, with adaptable and rigid regions coexisting.