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

Destabilization and stabilization of proteins.

John A Schellman1

  • 1Institute of Molecular Biology, University of Oregon, Eugene, OR 97405, USA. john@molbio.uoregon.edu

Quarterly Reviews of Biophysics
|March 11, 2006
PubMed
Summary

This study reviews how cosolvents stabilize or destabilize protein structures. A new application of solution theory confirms and expands these findings on protein unfolding and interactions.

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

In memoriam: Walter Kauzmann (1916-2009).

Protein science : a publication of the Protein Society·2010
Same author

Chemical potentials in a three-component, 1-dimensional liquid.

The journal of physical chemistry. B·2008
Same author

The Kauzmann lab in the late 1940s.

Biophysical chemistry·2003
Same author

Protein stability in mixed solvents: a balance of contact interaction and excluded volume.

Biophysical journal·2003
Same author

John T. Edsall: 3 November 1902-12 June, 2002.

Biophysical chemistry·2003
Same author

Fifty years of solvent denaturation.

Biophysical chemistry·2002

Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Chemical Thermodynamics

Background:

  • Protein conformation is crucial for biological function.
  • Cosolvents are widely used to study and manipulate protein stability.
  • Understanding protein-ligand interactions is key in drug discovery.

Purpose of the Study:

  • To provide a historical overview of protein conformation changes induced by cosolvents.
  • To apply the Kirkwood-Buff theory to generalize findings on protein stabilization/destabilization.
  • To derive formulas for preferential interaction and free energy of unfolding.

Main Methods:

  • Review of historical conceptual steps in protein conformation studies.
  • Application of the Kirkwood-Buff theory of solutions.
  • Derivation of theoretical formulas for thermodynamic properties.

Main Results:

  • Established distinct conceptual steps in protein stabilization/destabilization by cosolvents.
  • Derived generalized formulas for preferential interaction.
  • Derived generalized formulas for the free energy of unfolding.
  • Confirmed and extended previous findings using a theoretical framework.

Conclusions:

  • The Kirkwood-Buff theory provides a robust framework for understanding cosolvent effects on proteins.
  • Theoretical insights confirm and generalize empirical observations on protein unfolding.
  • This work offers a unified approach to cosolvent-protein interactions.

Related Experiment Videos