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 structures under electrospray conditions.

Alexandra Patriksson1, Erik Marklund, David van der Spoel

  • 1Department of Cell and Molecular Biology, Uppsala University, Husargatan 3, Box 596, SE-751 24 Uppsala, Sweden.

Biochemistry
|January 24, 2007
PubMed
Summary
This summary is machine-generated.

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

Bayesian Modeling of Polarizable Water: Lessons for Force Field Development.

Journal of chemical theory and computation·2026
Same author

LacI strikes a balance between stability and inducibility.

Nucleic acids research·2026
Same author

plotXVG: Batch Generation of Publication-Quality Graphs from GROMACS Output.

Journal of chemical information and modeling·2026
Same author

Beyond Partitioning: Using Force Field Science to Evaluate Electrostatics Models.

Journal of chemical theory and computation·2026
Same author

Correction to "Impact of Combination Rules, Level of Theory, and Potential Function on the Modeling of Gas- and Condensed-Phase Properties of Noble Gases".

Journal of chemical theory and computation·2025
Same author

Point + Gaussian charge model for electrostatic interactions derived by machine learning.

Physical chemistry chemical physics : PCCP·2025
Same journal

Structural and Functional Characterization of Heterologous Nitrogenase Complexes.

Biochemistry·2026
Same journal

Discovery of Bacterial Unspecific Peroxygenases.

Biochemistry·2026
Same journal

Lactate Biology: Subcellular Routing and Chemical Form Define Function.

Biochemistry·2026
Same journal

Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.

Biochemistry·2026
Same journal

Structural Bases for the Unconventional Activity of a Viroporin Channel.

Biochemistry·2026
Same journal

Targeting the WASF3 Regulatory Complex in Pancreatic Cancer Using Stapled Peptides.

Biochemistry·2026
See all related articles

Computer simulations reveal how proteins change conformation during electrospray ionization (ESI) from solution to vacuum. While major protein features are preserved, dehydration alters structures, favoring intramolecular bonds and exposing hydrophobic areas.

Area of Science:

  • Computational chemistry
  • Biophysics
  • Protein science

Background:

  • Electrospray ionization (ESI) transfers proteins from solution to vacuum, potentially altering their conformation.
  • Experimental determination of protein structural changes during dehydration is challenging.

Purpose of the Study:

  • To monitor protein structural changes during gradual evaporation of surrounding water using computer simulations.
  • To understand the effects of dehydration on protein conformation during the transition from solution to vacuum.

Main Methods:

  • Simulated the transition of five different proteins from water to vacuum using varying water shell thicknesses.
  • Monitored protein structure evolution throughout the dehydration process.

Main Results:

Related Experiment Videos

  • All simulated protein structures were affected by the transfer, but major features were preserved.
  • A water shell of approximately two molecules effectively emulates bulk water, maintaining solution-phase structure.
  • Vacuum conformations formed an ensemble differing from experimental and solution-phase structures.
  • Dehydration increased intramolecular hydrogen bonds and exposed more hydrophobic surface area.

Conclusions:

  • Native hydrogen bonds generally persist in vacuum, facilitating refolding upon rehydration.
  • Findings support the use of mass spectrometry for studying intra- and intermolecular interactions.
  • Results are promising for future bio-imaging experiments, such as with X-ray free electron lasers.