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

19.2K
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...
19.2K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

2.8K
2.8K
Personality Disorders: Dependent and Obsessive-Compulsive01:24

Personality Disorders: Dependent and Obsessive-Compulsive

418
Dependent personality disorder and obsessive-compulsive personality disorder are two separate psychological conditions that influence behavior, relationships, and overall life functioning. Though both involve maladaptive behaviors, their core characteristics and motivations differ significantly.
 Dependent Personality Disorder
Dependent personality disorder is characterized by an excessive reliance on others to manage various aspects of life. Individuals with this disorder often struggle...
418
Solvents01:12

Solvents

70.1K
A solvent is a substance, most often a liquid, that can dissolve other substances. Here, the substance being dissolved is called a solute. When a solvent and a solute combine, they form a solution - a homogenous mixture of both the solvent and the solute. Water is a universal biological solvent. Its polar structure allows it to dissolve many other polar compounds. The ability of water to dissolve is governed by a balance between water molecules binding to each other and binding to the solute.
A...
70.1K
Contact-dependent Signaling01:19

Contact-dependent Signaling

46.9K
Contact-dependent signaling, as the name suggests, requires that communicating cells be in direct contact with each other. This is achieved either through receptor-ligand interactions or by specialized cytoplasmic channels that allow the flow of small molecules between cells. In animal cells, channels called gap junctions facilitate contact-dependent signaling in certain tissues, whereas, plasmodesmata perform a similar function in plants.
Gap Junctions
In animal cells, gap junctions are formed...
46.9K
Titration in Nonaqueous Solvents01:16

Titration in Nonaqueous Solvents

1.4K
Most acid-base titrations are performed in an aqueous medium. In aqueous titrations, water competes with weaker acids or bases for proton donation or acceptance, leading to ambiguous endpoints in the titration curve. Water also affects the partial ionization of weak acids or bases. For example, water accepts a proton from acetic acid to form hydronium and acetate ions. The hydronium ion formed is a stronger acid than acetic acid, and the acetate ion is a stronger base than water. As a result,...
1.4K

You might also read

Related Articles

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

Sort by
Same author

Fibril Structure of Desiccation-Protective Tardigrade Protein CAHS-8.

Angewandte Chemie (International ed. in English)·2025
Same author

Structures of influenza A and B replication complexes give insight into avian to human host adaptation and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase.

Nature communications·2024
Same author

A specific phosphorylation-dependent conformational switch in SARS-CoV-2 nucleocapsid protein inhibits RNA binding.

Science advances·2024
Same author

Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro.

Nature structural & molecular biology·2024
Same author

Intrinsically disordered regions in TRPV2 mediate protein-protein interactions.

Communications biology·2023
Same author

Multivalent Dynamic Colocalization of Avian Influenza Polymerase and Nucleoprotein by Intrinsically Disordered ANP32A Reveals the Molecular Basis of Human Adaptation.

Journal of the American Chemical Society·2023
Same journal

Taphonomic analysis at Liang Bua reveals the behavioral and technological capabilities of <i>Homo floresiensis</i>.

Science advances·2026
Same journal

Targeting granule initiation and amyloplast structure to create giant starch granules in wheat.

Science advances·2026
Same journal

A meta-analysis of carbon losses and gains from tropical moist forest degradation and regeneration.

Science advances·2026
Same journal

Ancient DNA reveals elite dynastic rule among Iron Age Eurasian Steppe nomads.

Science advances·2026
Same journal

Targeting astrocytic Dp71 attenuates BBB disruption after traumatic brain injury through WTAP-associated m<sup>6</sup>A regulation of MMP2.

Science advances·2026
Same journal

Pancreatic α cells are required for nutrient homeostasis by regulating dynamic β cell networks in islets.

Science advances·2026
See all related articles

Related Experiment Video

Updated: Jan 22, 2026

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

2.2K

Solvent-dependent segmental dynamics in intrinsically disordered proteins.

Nicola Salvi1, Anton Abyzov1, Martin Blackledge1

  • 1UniversitĂ© Grenoble Alpes, CNRS, CEA, IBS, 38000 Grenoble, France.

Science Advances
|July 2, 2019
PubMed
Summary
This summary is machine-generated.

Water dynamics are crucial for the internal motion of intrinsically disordered proteins (IDPs). Understanding this protein-water coupling, including hydrogen bond lifetimes, is key for accurate protein relaxation studies.

More Related Videos

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

19.4K
Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

9.4K

Related Experiment Videos

Last Updated: Jan 22, 2026

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

2.2K
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

19.4K
Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

9.4K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Biology

Background:

  • Protein and water dynamics exhibit a synergistic relationship, vital for intrinsically disordered proteins (IDPs).
  • The precise coupling between protein and solvent motion in IDPs remains incompletely understood.
  • Intrinsically disordered proteins lack stable tertiary structures, making their dynamics highly flexible and solvent-dependent.

Purpose of the Study:

  • To investigate the role of distinct solvent and solute motion modes in accurately reproducing site-specific dynamics of IDPs.
  • To elucidate the coupling between water dynamics and internal protein motions within IDPs.
  • To establish a link between intrasegmental dynamics timescales and bulk water hydrogen bond lifetimes.

Main Methods:

  • Utilized temperature-dependent molecular dynamics simulations with various water models.
  • Employed extensive nuclear magnetic resonance (NMR) relaxation measurements.
  • Analyzed site-specific dynamics and correlated them with solvent properties.

Main Results:

  • Water dynamics significantly influence motional processes within "segments" of IDPs.
  • Identified a direct relationship between intrasegment dynamics timescales and hydrogen bond lifetimes in bulk water.
  • Demonstrated that accurate modeling of these motions is essential for reproducing protein relaxation data.

Conclusions:

  • Water dynamics are integral to the functional dynamics of intrinsically disordered proteins.
  • The findings highlight the critical role of hydration water in the behavior and function of IDPs.
  • This study provides new perspectives on the interplay between protein structure, dynamics, and hydration in biological systems.