Jove
Visualize
Contact Us

Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

19.1K
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...
19.1K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

2.7K
2.7K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.4K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.4K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.3K
4.3K
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

62.9K
Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
62.9K
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

19.1K
19.1K

You might also read

Related Articles

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

Sort by
Same author

Macromolecular crowding reshapes the conformational landscapes of intrinsically disordered proteins: mechanisms, cellular contexts, and functional consequences.

Current opinion in structural biology·2026
Same author

Force Field Evaluation for an Intrinsically Disordered Domain: MD-NMR-FCS Benchmarking of Protein 4.1G Headpiece Ensembles.

Journal of chemical information and modeling·2026
Same author

Improvement of Output Characteristics of Dual-Loss-Modulated Laser with Heterostructure Saturable Absorber at 1.3 μm.

Materials (Basel, Switzerland)·2026
Same author

Computing Paramagnetic <sup>13</sup>C NMR Chemical Shifts of Cobalt(II) Porphyrins with the eXtended ONIOM Method.

Journal of chemical theory and computation·2026
Same author

Bacillus-Derived Lipopeptides as Green Biosurfactants: Structures, Functions, Production, and Safety for Sustainable Applications.

Comprehensive reviews in food science and food safety·2026
Same author

LiteMapNet: Lightweight Online High-Definition Mapping With Attention Head Pruning.

Annals of the New York Academy of Sciences·2026
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 Experiment Video

Updated: Jan 2, 2026

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

2.6K

Dynamic multivalent interactions of intrinsically disordered proteins.

Jingwei Weng1, Wenning Wang1

  • 1Multiscale Research Institute of Complex Systems, Department of Chemistry and Institute of Biomedical Sciences, Fudan University, Shanghai, PR China.

Current Opinion in Structural Biology
|November 30, 2019
PubMed
Summary

Intrinsically disordered proteins (IDPs) engage in dynamic, multivalent interactions (DMIs) crucial for various functions. Characterizing these complex interactions requires integrating multiple experimental techniques with microscopic modeling to understand binding thermodynamics and kinetics.

More Related Videos

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

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

Published on: September 23, 2021

2.1K
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.4K

Related Experiment Videos

Last Updated: Jan 2, 2026

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

2.6K
Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

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

Published on: September 23, 2021

2.1K
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.4K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Intrinsically disordered proteins (IDPs) are key players in cellular processes.
  • IDPs exhibit dynamic and multivalent interactions (DMIs) essential for their functions.
  • The complex and promiscuous nature of DMIs presents significant characterization challenges.

Purpose of the Study:

  • To highlight the functional significance of DMIs in intrinsically disordered proteins.
  • To underscore the challenges in characterizing the dynamic and multivalent nature of IDP interactions.
  • To emphasize the necessity of integrated approaches for elucidating DMI mechanisms.

Main Methods:

  • Review of recent experimental data on IDP interactions.
  • Discussion of the complexities in characterizing DMI.
  • Emphasis on the combined use of various techniques.
  • Introduction of microscopic models for binding thermodynamics and kinetics.

Main Results:

  • DMIs of IDPs are functionally significant across various biological contexts.
  • Characterizing DMIs is inherently challenging due to their dynamic and promiscuous properties.
  • Successful elucidation of DMI mechanisms necessitates a multidisciplinary approach.

Conclusions:

  • Understanding the mechanistic role of DMI in IDPs is critical.
  • Integrated experimental and computational strategies are essential for characterizing DMI.
  • Future research should focus on combining techniques and microscopic models to unravel DMI thermodynamics and kinetics.