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

You might also read

Related Articles

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

Sort by
Same author

Integrated structural dynamics uncover a new B<sub>12</sub> photoreceptor activation mode.

Nature·2026
Same author

BindFlow: A Free, User-Friendly Pipeline for Absolute Binding Free Energy Calculations Using Free Energy Perturbation or MM(PB/GB)SA.

Journal of chemical theory and computation·2026
Same author

Depletion of the Protein Hydration Shell with Increasing Temperature Observed by Small-Angle X-ray Scattering and Molecular Simulations.

Journal of the American Chemical Society·2025
Same author

Depletion of the protein hydration shell with increasing temperature observed by small-angle X-ray scattering and molecular simulations.

bioRxiv : the preprint server for biology·2025
Same author

How pore formation in complex biological membranes is governed by lipid composition, mechanics, and lateral sorting.

PNAS nexus·2025
Same author

Structural insights into tecovirimat antiviral activity and poxvirus resistance.

Nature microbiology·2025

Related Experiment Video

Updated: Jul 8, 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

1.8K

Scrutinizing the protein hydration shell from molecular dynamics simulations against consensus small-angle scattering

Johanna-Barbara Linse1, Jochen S Hub2

  • 1Theoretical Physics and Center for Biophysics, Saarland University, Saarbrücken, 66123, Germany.

Communications Chemistry
|December 12, 2023
PubMed
Summary

Small-angle scattering reveals how protein shape and charge influence their hydration shell structure. This provides a new way to test computer models of protein-water interactions against experimental data.

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

10.6K
Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
11:14

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders

Published on: April 14, 2015

16.1K

Related Experiment Videos

Last Updated: Jul 8, 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

1.8K
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

10.6K
Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
11:14

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders

Published on: April 14, 2015

16.1K

Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Biology

Background:

  • Biological macromolecules possess a hydration shell, distinct from bulk solvent, crucial for biological functions.
  • Understanding hydration shell regulation by macromolecular shape and surface properties is limited by a lack of quantitative probes.

Purpose of the Study:

  • To establish small-angle scattering (SAXS/SANS) as a protein-specific probe for hydration shell structure.
  • To enable quantitative comparison between experimental hydration shell data and molecular simulations.

Main Methods:

  • Utilized explicit-solvent small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS) predictions.
  • Calculated the effect of hydration shells on the radius of gyration (Rg) for five proteins using 18 force field/water model combinations.
  • Compared computed Rg values with consensus experimental SAXS/SANS data.

Main Results:

  • Several protein force fields and water models accurately predicted experimental hydration shell contrast.
  • The hydration shell's influence on Rg is strongly dependent on protein charge and geometric shape.
  • SAXS/SANS provide a protein-specific footprint of protein-water interactions.

Conclusions:

  • Small-angle scattering offers a novel observable for validating atomistic hydration shell models.
  • Protein shape and surface properties significantly dictate hydration shell characteristics.
  • This approach advances the quantitative understanding of protein hydration in solution.