Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Diffusion in the Membrane

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...

Entropy and Solvation

Entropy and Solvation

The process of surrounding a solute with solvent is called solvation. It involves evenly distributing the solute within the solvent. The rule of thumb for determining a solvent for a given compound is that like dissolves like. A good solvent has molecular characteristics similar to those of the compound to be dissolved. For example, polar solutions dissolve polar solutes, and apolar solvents dissolve apolar solutes. A polar solvent is a solvent that has a high dielectric constant (ϵ ≥ 15); an...

Intermolecular Forces

Intermolecular Forces

Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen bonds, and dispersion...

Aquaporins

Aquaporins

Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.

Aqueous Solutions and Heats of Hydration

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...

Solubility

Solubility

Solution, Solubility, and Solubility Equilibrium
A solution is a homogeneous mixture composed of a solvent, the major component, and a solute, the minor component. The physical state of a solution—solid, liquid, or gas—is typically the same as that of the solvent. Solute concentrations are often described with qualitative terms such as dilute (of relatively low concentration) and concentrated (of relatively high concentration).
In a solution, the solute particles (molecules, atoms, and/or ions)...

You might also read

Related Articles

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

Sort by

Same author

Solvent-Mediated Control of Nanocellulose Dispersion: An Integrated Computational and Experimental Investigation.

ACS nano·2026

Same author

The scientific legacy of Martin Karplus from the perspective of his collaborators.

Biophysical journal·2026

Same author

IRIS: A Machine Learning-Based Pose Reranking Tool for RNA-Ligand Docking.

ACS omega·2026

Same author

Allosteric prediction via convolutional neural networks and protein structural and dynamical features.

Biophysical journal·2025

Same author

Simulation and generalized Langevin equation study of lipid subdiffusion in biomembrane phases.

Biophysical journal·2025

Same author

Divergent responses of branched and straight-chain lipid membranes to butanol stress revealed by molecular dynamics simulation.

Biophysical journal·2025

Search research articles

Related Experiment Video

Updated: May 18, 2026

In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS

In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS

Published on: February 15, 2016

Surface hydration amplifies single-well protein atom diffusion propagating into the macromolecular core.

Liang Hong¹, Xiaolin Cheng, Dennis C Glass

¹UT/ORNL Center for Molecular Biophysics, Oak Ridge National Laboratory, P.O. Box 2008, Oak Ridge, Tennessee 37831, USA.

Physical Review Letters

|September 26, 2012

Summary

Surface hydration significantly impacts protein dynamics by increasing localized atomic diffusion. This effect, crucial for molecular biophysics, propagates from the protein surface inward, influencing internal motions.

More Related Videos

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Related Experiment Videos

Last Updated: May 18, 2026

In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS

In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS

Published on: February 15, 2016

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Area of Science:

Molecular Biophysics
Computational Biology
Protein Dynamics

Background:

Understanding protein internal motion is key to molecular biophysics.
Surface hydration's role in protein dynamics remains an area of fundamental interest.
Atomic-level motions within proteins are influenced by their surrounding environment.

Purpose of the Study:

To investigate the effect of surface hydration on the internal atomic motion of proteins.
To quantify how different hydration levels alter protein dynamics.
To elucidate the mechanisms by which hydration influences protein flexibility.

Main Methods:

Utilized molecular dynamics simulations of lysozyme at various hydration levels.
Decomposed atomic motion into localized single-well diffusion, methyl group rotation, and nonmethyl jumps.
Analyzed picosecond to nanosecond timescale atomic movements.

Main Results:

Surface hydration primarily increases the volume of localized single-well diffusion.
Hydration-induced diffusive motions are coupled, affecting the entire protein.
The influence of surface hydration extends from the protein surface to its core.

Conclusions:

Surface hydration plays a critical role in modulating protein internal dynamics.
Localized diffusion is the primary motion affected by hydration levels.
Hydration effects propagate through the protein structure, impacting core flexibility.