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

Solvent structure at a hydrophobic protein surface

H Kovacs1, A E Mark, W F van Gunsteren

  • 1Laboratory of Physical Chemistry, Swiss Federal Institute of Technology Zürich, Switzerland.

Proteins
|March 1, 1997
PubMed
Summary

Hydrophobic protein surfaces disrupt water structure, contrary to the hydrophobic effect model. Solvent behavior is complex and depends on local environments, not just solvent polarity.

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

Effect of pH and lipopolysaccharide on tight junction regulators and inflammatory markers in intestinal cells as an experimental model of weaning transition in dairy calves.

JDS communications·2023
Same author

Parametrisation of time-averaged distance restraints in MD simulations.

Journal of biomolecular NMR·2012
Same author

Investigations of peptide hydration using NMR and molecular dynamics simulations: A study of effects of water on the conformation and dynamics of antamanide.

Journal of biomolecular NMR·2010
Same author

Molecular dynamics simulation using weak-coupling NOE distance restraining.

Journal of biomolecular NMR·2010
Same author

On using time-averaging restraints in molecular dynamics simulation.

Journal of biomolecular NMR·2009
Same author

Temperature and urea induced denaturation of the TRP-cage mini protein TC5b: A simulation study consistent with experimental observations.

Protein science : a publication of the Protein Society·2009

Area of Science:

  • Biophysics
  • Physical Chemistry
  • Computational Biology

Background:

  • The hydrophobic effect is a key concept in molecular biology, explaining protein folding and self-assembly.
  • Current models suggest enhanced water structuring at hydrophobic interfaces.
  • This study investigates solvent behavior at protein surfaces.

Purpose of the Study:

  • To investigate the impact of hydrophobic protein surfaces on surrounding solvent structure.
  • To test the hypothesis of enhanced water structuring at hydrophobic interfaces.
  • To analyze solvent residence times and radial distribution functions.

Main Methods:

  • Molecular dynamics simulations of alpha-helical polypeptides (SP-C and titin) in various solvents (water, methanol, chloroform).
  • Analysis of solvent residence times and radial distribution functions around different atomic sites (methyl, polar, charged).
  • Comparison of solvent behavior across different polarities and surface charge distributions.

Main Results:

  • Hydrophobic protein surfaces disrupt, rather than enhance, water structure, showing no positional correlation beyond the first solvation sphere.
  • No clear trend was observed for more polar solvents being more ordered.
  • Solvent residence times showed no significant differences between nonpolar, polar, or charged sites, but were affected by the local environment.

Conclusions:

  • The hydrophobic effect may not be explained by enhanced water structuring at hydrophobic interfaces.
  • Solvent behavior at protein surfaces is complex and influenced by local atomic environments.
  • Further research is needed to fully understand the mechanisms of the hydrophobic effect.

Related Experiment Videos