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 Experiment Videos

Protein hydration dynamics in solution: a critical survey.

Bertil Halle1

  • 1Department of Biophysical Chemistry, Lund University, SE-22100 Lund, Sweden. bertil.halle@bpc.lu.se

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|August 13, 2004
PubMed
Summary

Protein hydration water is highly mobile, moving only twice as slow as bulk water. This mobility is crucial for biological processes like binding and catalysis at protein surfaces.

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

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

Compressibility of the protein-water interface.

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
Same author

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

The Journal of chemical physics·2016

Area of Science:

  • Biophysics
  • Physical Chemistry
  • Structural Biology

Background:

  • Protein hydration, the interaction between water and protein surfaces, remains poorly understood.
  • Previous studies on water dynamics near proteins yielded controversial and conflicting results.

Purpose of the Study:

  • To critically analyze existing concepts of protein hydration dynamics.
  • To evaluate the experimental evidence supporting current models of protein hydration.

Main Methods:

  • Oxygen-17 magnetic relaxation dispersion (MRD) experiments.
  • Comparison with data from molecular dynamics simulations, nuclear Overhauser effect spectroscopy, dielectric relaxation, and fluorescence spectroscopy.

Main Results:

Related Experiment Videos

  • MRD experiments reveal that protein hydration water is only twofold slower than bulk water.
  • This high mobility supports rapid protein-water interface processes like binding and catalysis.
  • Discrepancies with other spectroscopic methods and hydrodynamic models are addressed.
  • Conclusions:

    • The protein hydration layer exhibits significantly higher mobility than previously assumed.
    • This dynamic picture reconciles conflicting experimental data and theoretical models.
    • High hydration water mobility is essential for efficient biological functions at the protein surface.