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

Protein Folding01:22

Protein Folding

125.6K
Overview
125.6K
Protein Folding01:25

Protein Folding

10.7K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
10.7K
Factors Affecting Activity Coefficient01:17

Factors Affecting Activity Coefficient

1.4K
The extended Debye-Hückel equation indicates that the activity coefficient of an ion in an aqueous solution at 25°C depends on three partially interdependent properties: the ionic strength of the solution, the charge of the ion, and the ion size. 
The activity coefficient value for an ion is close to one when the solution has almost zero ionic strength, i.e., when the solution shows close to ideal behavior. As the ionic strength of the solution increases from 0 to 0.1 mol/L, a...
1.4K
Entropy and Solvation02:05

Entropy and Solvation

8.1K
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...
8.1K
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

62.8K
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,...
62.8K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

13.9K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
13.9K

You might also read

Related Articles

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

Sort by
Same author

Molecular Mechanisms of KIT Receptor Dimerization and Oncogenic Activation Revealed by Multiscale Simulations.

Journal of chemical information and modeling·2026
Same author

Water-modulated conformational heterogeneity underlies multiple timescales of primary charge separation in photosystem II.

Nature communications·2026
Same author

A general hydrogen-bond connectivity descriptor based on graph theory.

Physical chemistry chemical physics : PCCP·2026
Same author

Theoretical-computational modeling of the vibrational chirality of interacting chromophores: VCD signal and equilibrium properties of excitonic clusters.

The Journal of chemical physics·2026
Same author

A computational approach for the calculation of two-dimensional infrared spectra: Application to the amide I band.

The Journal of chemical physics·2026
Same author

Molecular Dynamics Workflows to Compute Large-Scale Sets of Absolute Binding Free Energies Aiding Drug Candidate and Binding Pose Selection.

Journal of chemical theory and computation·2026

Related Experiment Video

Updated: Dec 25, 2025

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

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

Published on: April 28, 2022

2.0K

Length-scale dependence of protein hydration-shell density.

Akash Deep Biswas1, Vincenzo Barone, Andrea Amadei

  • 1Department of Physical and Chemical Sciences, University of L'Aquila, via Vetoio (Coppito 1), 67010 L'Aquila, Italy. isabella.daidone@univaq.it.

Physical Chemistry Chemical Physics : PCCP
|March 27, 2020
PubMed
Summary

Protein size significantly impacts hydration shell density. Larger proteins show a higher density increase, primarily within internal pockets, a finding consistent across various protein types.

More Related Videos

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
09:49

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Published on: April 2, 2015

10.9K
Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
06:48

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

5.0K

Related Experiment Videos

Last Updated: Dec 25, 2025

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

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

Published on: April 28, 2022

2.0K
Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
09:49

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Published on: April 2, 2015

10.9K
Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
06:48

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

5.0K

Area of Science:

  • Computational biophysics
  • Structural biology
  • Biomolecular simulations

Background:

  • Protein hydration shells are crucial for molecular interactions and stability.
  • Understanding hydration shell density variations is key to deciphering protein behavior.

Purpose of the Study:

  • To investigate the relationship between protein size and hydration shell density.
  • To quantify hydration shell density changes across diverse protein molecules.
  • To explore the influence of protein size on water molecule distribution.

Main Methods:

  • Utilized molecular dynamics (MD) simulations for computational analysis.
  • Calculated hydration shell density for eighteen proteins of varying sizes and functions.
  • Developed a simplified model approximating proteins as ellipsoids to analyze density distribution.

Main Results:

  • Observed a 4-14% increase in hydration shell density relative to bulk water for all proteins studied.
  • Demonstrated a strong positive correlation between protein size and hydration shell density increment.
  • Found that the density increase is predominantly located within internal protein pockets or at the protein surface.
  • Noted that protein size, not protein type (antifreeze vs. non-antifreeze), drives density changes.

Conclusions:

  • Protein size is the primary determinant of hydration shell density variations.
  • The observed density increments are largely confined to the protein's internal structure.
  • The computational model effectively explains the size-dependent hydration shell density phenomenon.