Jove
Visualize
Contact Us

Related Experiment Videos

Modeling charge interactions and redox properties in DsbA

J Warwicker1

  • 1Institute of Food Research, Reading Laboratory, Earley Gate, Whiteknights Road, Reading RG6 6BZ, United Kingdom.

The Journal of Biological Chemistry
|February 28, 1998
PubMed
Summary

Computational biology models for DsbA protein charge interactions were tested. Experimental data align with the model, showing multiple factors contribute to DsbA’s oxidizing power.

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

Polyunsaturated fatty acids inhibit Kv1.4 by interacting with positively charged extracellular pore residues.

American journal of physiology. Cell physiology·2016
Same author

Specific ion and buffer effects on protein-protein interactions of a monoclonal antibody.

Molecular pharmaceutics·2014
Same author

The role of electrostatics in protein-protein interactions of a monoclonal antibody.

Molecular pharmaceutics·2014
Same author

Freezing and folding behavior in simple off-lattice heteropolymers.

The Journal of chemical physics·2004
Same author

Biochemical and genetic evidence for a family of heterotrimeric G-proteins in Trichomonas vaginalis.

Molecular and biochemical parasitology·2003
Same author

A second eIF4E protein in Schizosaccharomyces pombe has distinct eIF4G-binding properties.

Nucleic acids research·2001
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

Area of Science:

  • Computational biology
  • Protein biophysics
  • Biochemistry

Background:

  • Accurate prediction of charge interactions in macromolecules is crucial but challenging.
  • A previously developed model explained the low Cys30 pKa and oxidizing power of DsbA.
  • Experimental investigations of DsbA mutants (Glu37, Glu38 substitutions, residue 38-40 deletion) yielded results seemingly contrasting model predictions.

Purpose of the Study:

  • To re-evaluate experimental data in light of the DsbA model.
  • To demonstrate consistency between experimental findings and the theoretical model.
  • To clarify the contributions of various factors to DsbA's oxidizing power.

Main Methods:

  • Computational modeling of DsbA wild-type and mutant proteins.
  • Analysis of experimental data for DsbA mutants across varying salt concentrations.
  • Comparison of calculated wild-type:mutant differences with experimental measurements.

Main Results:

  • Calculations of wild-type:mutant differences, particularly across salt concentrations, align with experimental data.
  • The findings support the model's assertion that multiple factors contribute to DsbA's oxidizing power.
  • A low protein dielectric, a key feature of the model, is consistent with the data, while higher values are not.

Conclusions:

  • Experimental data for DsbA mutants are consistent with the established computational model.
  • The study reinforces that DsbA's oxidizing power arises from a combination of factors.
  • The model's prediction of a low protein dielectric is supported, contradicting higher dielectric values often used in pH-dependent predictions.

Related Experiment Videos