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

Probing protein folding and stability using disulfide bonds

N Darby1, T E Creighton

  • 1European Molecular Biology Lab, Heidelberg, Germany.

Molecular Biotechnology
|February 1, 1997
PubMed
Summary

Disulfide bonds stabilize protein structures. Studying their formation and breakage rates provides key insights into protein folding and stability through various experimental methods.

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

Contributions of substrate binding to the catalytic activity of DsbC.

Biochemistry·1998
Same author

Protein folding coupled to disulphide bond formation.

Biological chemistry·1997
Same author

Protein folding: does diffusion determine the folding rate?

Current biology : CB·1997
Same author

The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules.

Current biology : CB·1997
Same author

How important is the molten globule for correct protein folding?

Trends in biochemical sciences·1997
Same author

Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase.

Biochemistry·1996

Area of Science:

  • Biochemistry
  • Protein Science
  • Structural Biology

Background:

  • Disulfide bonds are crucial covalent linkages that stabilize the three-dimensional structures of numerous proteins.
  • The dynamic processes of disulfide bond formation and breakage are integral to protein folding and conformational stability.

Purpose of the Study:

  • To describe experimental procedures for investigating disulfide bond dynamics.
  • To present approaches for interpreting data related to disulfide bond formation and breakage.
  • To highlight the utility of studying these processes for understanding protein folding and stability.

Main Methods:

  • Experimental manipulation of disulfide bond formation and breakage rates and equilibria.
  • Application of various biochemical and biophysical techniques to monitor disulfide bond status.
  • Data analysis methodologies for interpreting kinetic and equilibrium measurements.

Main Results:

  • Demonstration that rates and equilibria of disulfide bond processes are experimentally controllable.
  • Establishment of a link between disulfide bond dynamics and protein folding pathways.
  • Validation of experimental approaches for probing protein stability.

Conclusions:

  • Experimental study of disulfide bond dynamics offers valuable insights into protein folding and stability.
  • The described methods provide a framework for investigating protein conformational transitions.
  • Understanding disulfide bond manipulation is key for protein engineering and therapeutic development.

Related Experiment Videos