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-protein Interfaces

Protein-protein Interfaces

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...

Protein-Protein Interfaces

Protein-Protein Interfaces

States of Water

States of Water

Water exists in any one of the three classical states: solid (ice), liquid (water), and gas (steam or water vapor). The state of water depends on i) the intermolecular forces that draw molecules together and ii) the kinetic energy that leads to movements that pull them apart.
Water freezes when the intermolecular forces are greater than the kinetic energy. Unlike most other substances, water is less dense in its solid state than in its liquid state. This is because each water molecule can form...

Behavior of Concrete Under Compressive Load

Behavior of Concrete Under Compressive Load

Concrete exhibits specific behaviors under different compressive loads. Understanding this is crucial for understanding its structural integrity. When concrete undergoes uniaxial compression, it tends to develop cracks that run parallel to the direction of the force. These parallel cracks stem from localized tensile stresses that occur perpendicular to the compression direction. Additionally, angled cracks may appear due to the formation of shear planes.
As the concrete specimen fractures under...

The Water Cycle

The Water Cycle

The Earth’s hydrosphere includes all of the areas where the storage and movement of water occurs. Since water is the basis of all living processes, the cycling of water is extremely important to ecosystem dynamics.

Water and Mineral Acquisition

Water and Mineral Acquisition

Specialized tissues in plant roots have evolved to capture water, minerals, and some ions from the soil. Roots exhibit a variety of branching patterns that facilitate this process. The outermost root cells have specialized structures called root hairs that increase the root surface, thus increasing soil contact. Water can passively cross into roots, as the concentration of water in the soil is higher than that of the root tissue. Minerals, in contrast, are actively transported into root cells.

You might also read

Related Articles

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

Sort by

Same author

How proteins modify water dynamics.

The Journal of chemical physics·2018

Same author

The spatial range of protein hydration.

The Journal of chemical physics·2018

Same author

The geometry of protein hydration.

The Journal of chemical physics·2018

Same author

Nuclear magnetic relaxation by the dipolar EMOR mechanism: Multi-spin systems.

The Journal of chemical physics·2017

Search research articles

Related Experiment Video

Updated: Feb 9, 2026

Dissolved Solute Sampling Across an Oxic-Anoxic Soil-Water Interface Using Microdialysis Profilers

Dissolved Solute Sampling Across an Oxic-Anoxic Soil-Water Interface Using Microdialysis Profilers

Published on: March 24, 2023

Compressibility of the protein-water interface.

Filip Persson¹, Bertil Halle¹

¹Division of Biophysical Chemistry, Department of Chemistry, Lund University, P.O. Box 124, SE-22100 Lund, Sweden.

The Journal of Chemical Physics

|June 10, 2018

Summary

Protein compressibility, crucial for stability and flexibility, is challenging to measure and compute. Our study reveals protein-water volume fluctuations significantly influence protein compressibility, with hydration shells showing reduced intrinsic compressibility near the protein surface.

More Related Videos

Author Spotlight: Advancing Understanding of Age-Related Lens Stiffness Changes

Author Spotlight: Advancing Understanding of Age-Related Lens Stiffness Changes

Published on: April 5, 2024

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

Related Experiment Videos

Last Updated: Feb 9, 2026

Dissolved Solute Sampling Across an Oxic-Anoxic Soil-Water Interface Using Microdialysis Profilers

Dissolved Solute Sampling Across an Oxic-Anoxic Soil-Water Interface Using Microdialysis Profilers

Published on: March 24, 2023

Author Spotlight: Advancing Understanding of Age-Related Lens Stiffness Changes

Author Spotlight: Advancing Understanding of Age-Related Lens Stiffness Changes

Published on: April 5, 2024

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

Area of Science:

Biophysics
Thermodynamics
Computational Biology

Background:

Protein compressibility is a key thermodynamic parameter linked to stability, flexibility, and hydrophobic interactions.
Measuring, interpreting, and computing protein compressibility face significant technical and conceptual hurdles.

Purpose of the Study:

To theoretically analyze protein compressibility and apply this analysis to molecular dynamics simulations.
To decompose solution compressibility into protein and hydration shell contributions.
To investigate the contributions of protein-water volume fluctuations and hydration shell properties to overall protein compressibility.

Main Methods:

Theoretical analysis of protein compressibility.
Molecular dynamics simulations of four globular proteins.
Additively weighted Voronoi tessellation for decomposing solution compressibility.
Analysis of protein-water volume fluctuations and hydration shell properties.

Main Results:

Positively cross-correlated protein-water volume fluctuations contribute over half of the protein compressibility governing pressure response.
The total protein compressibility, including cross-correlations, is approximately 45% of the bulk-water value.
Intrinsic hydration shell compressibility is 25%-30% lower than bulk water, primarily due to proximity to the protein.

Conclusions:

Protein compressibility is significantly influenced by protein-water interactions and hydration shell properties.
The study provides a framework for computing protein partial compressibility, distinguishing intrinsic, hydration, and exchange contributions.
Hydration shell compressibility is reduced near the protein surface, not due to altered water structure, but protein proximity.