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

Role of Water in Human Biology01:27

Role of Water in Human Biology

Water is the one of the most significant components of the human body; it plays a crucial role in several physiological activities because of its unique physicochemical properties. Importantly, it helps to regulate body temperature and is the chief component of several body fluids.
Water's Solvent Properties
Since water is a polar molecule with slightly positive and slightly negative charges, ions and polar molecules can readily dissolve in it. Therefore, it is referred to as a solvent, a...
Fluid Movement Between Compartments01:18

Fluid Movement Between Compartments

The force applied by fluids against a surface, known as hydrostatic pressure, initiates the transfer of fluid among different compartments. Within our blood vessels, the blood's hydrostatic pressure is a result of the heart's pumping action. At the arteriolar end of capillaries, hydrostatic pressure (capillary blood pressure) exceeds the opposing colloid osmotic pressure created primarily by plasma proteins like albumin. This discrepancy in pressure propels plasma and nutrients from the...
Aqueous Solutions and Heats of Hydration02:42

Aqueous Solutions and Heats of Hydration

Water and other polar molecules are attracted to ions. The electrostatic attraction between an ion and a molecule with a dipole is called an ion-dipole attraction. These attractions play an important role in the dissolution of ionic compounds in water.
When ionic compounds dissolve in water, the ions in the solid separate and disperse uniformly throughout the solution because water molecules surround and solvate the ions, reducing the strong electrostatic forces between them. This process...
Body Water Content and Fluid Compartments01:19

Body Water Content and Fluid Compartments

Life's biochemical processes occur within aqueous solutions. Solutes are substances that are dissolved within these solutions. The human body contains a variety of solutes, which can differ across various body parts. These can encompass proteins—such as those responsible for clotting and carbohydrate transport—as well as electrolytes. In medicine, an electrolyte is often described as a mineral ion derived from a salt possessing an electric charge. Examples include sodium ions (Na+) and chloride...
Solubility Equilibria: Ionic Product of Water01:16

Solubility Equilibria: Ionic Product of Water

Pure water is a weak electrolyte; only a small amount ionizes into hydrogen and hydroxide ions. At any given temperature, the concentration of undissociated water is almost constant, so the ionic product of water is the product of the hydrogen and hydroxide ion concentrations, denoted as Kw. The square root of Kw gives the individual ion concentrations.
The ionic product of water varies with temperature, and its value is 1.0 x 10−14 at standard experimental conditions. Per Le Chatelier's...
Water: A Bronsted-Lowry Acid and Base02:30

Water: A Bronsted-Lowry Acid and Base

The reaction between a Brønsted-Lowry acid and water is called acid ionization. For example, when hydrogen fluoride dissolves in water and ionizes, protons are transferred from hydrogen fluoride molecules to water molecules, yielding hydronium ions and fluoride ions:

You might also read

Related Articles

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

Sort by
Same author

Machine-Learned Leftmost Hessian Eigenvectors for Robust Transition State Finding.

Journal of chemical theory and computation·2026
Same author

Energetics of Noncovalent Interactions of Protein-Ligand Complexes for Drug Discovery.

Journal of chemical information and modeling·2026
Same author

Sensing the acidity of hydrogen bond networks.

Physical chemistry chemical physics : PCCP·2026
Same author

SmileyLlama: modifying large language models for directed chemical space exploration.

Nature computational science·2026
Same author

Conformational Ensembles of the Disordered 4E-BP2:eIF4E Complex Restrained by smFRET Experiments.

bioRxiv : the preprint server for biology·2026
Same author

LinkLlama: Enabling Large Language Model for Chemically Reasonable Linker Design.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Jun 23, 2026

Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy
10:28

Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy

Published on: May 27, 2018

Hydration water dynamics near biological interfaces.

Margaret E Johnson1, Cecile Malardier-Jugroot, Rajesh K Murarka

  • 1Department of Bioengineering, University of California, Berkeley, 94720, USA.

The Journal of Physical Chemistry. B
|May 9, 2009
PubMed
Summary

Molecular dynamics simulations reveal distinct hydration dynamics near amphiphilic peptides, explaining experimental observations. This suggests chemical heterogeneity, not just surface shape, drives water dynamics at biological interfaces.

More Related Videos

Temperature-Controlled Assembly and Characterization of a Droplet Interface Bilayer
10:11

Temperature-Controlled Assembly and Characterization of a Droplet Interface Bilayer

Published on: April 19, 2021

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

Related Experiment Videos

Last Updated: Jun 23, 2026

Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy
10:28

Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy

Published on: May 27, 2018

Temperature-Controlled Assembly and Characterization of a Droplet Interface Bilayer
10:11

Temperature-Controlled Assembly and Characterization of a Droplet Interface Bilayer

Published on: April 19, 2021

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

Area of Science:

  • Biophysics
  • Computational Chemistry
  • Physical Chemistry

Background:

  • Hydration dynamics near biological interfaces are crucial for protein function.
  • Understanding water's behavior at peptide and protein surfaces is key to molecular recognition and biological processes.
  • Previous studies suggest surface topology influences hydration, but the role of chemical heterogeneity is less clear.

Purpose of the Study:

  • To investigate and contrast hydration dynamics near hydrophilic and amphiphilic peptides using molecular dynamics simulations.
  • To model high peptide concentrations to simulate overlapping hydration layers found on folded protein surfaces.
  • To elucidate the origins of experimentally observed translational relaxations in peptide hydration layers.

Main Methods:

  • Classical molecular dynamics simulations were employed.
  • Both fixed-charge and polarizable water and protein force fields were utilized.
  • Simulations were conducted at varying temperatures to analyze hydration dynamics.

Main Results:

  • Amphiphilic peptide solutions exhibited distinct water dynamics between outer and inner hydration layers, correlating with two observed translational relaxations.
  • Hydrophilic peptide solutions showed a single, non-Arrhenius translational process without hydration layer differentiation.
  • The amphiphilic system's water dynamics successfully reproduced known hydration anomalies near protein surfaces.

Conclusions:

  • Differences in hydration dynamics near amphiphilic peptides arise from chemical heterogeneity, not solely topological roughness.
  • Frustration in hydration dynamics induced by chemical heterogeneity is a primary driver of dynamical signatures near biological interfaces.
  • These findings provide strong evidence for the role of chemical heterogeneity in shaping water dynamics at protein surfaces.