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Related Experiment Videos

Salt-promoted protein folding, preferential binding, or electrostatic screening?

Earle Stellwagen1, Erna Olivieri, Pier Giorgio Righetti

  • 1Department of Biochemistry, University of Iowa, Iowa City, Iowa 52242, USA. earle-stellwagen@uiowa.edu

Proteins
|September 5, 2002
PubMed
Summary

Ferricytochrome c

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Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Protein Science

Background:

  • Ferricytochrome c exhibits an extended coil/molten globule conformational equilibrium in acidic solutions.
  • Understanding protein conformational changes is crucial in biochemistry and biophysics.

Purpose of the Study:

  • To investigate the conformational equilibrium of ferricytochrome c in acidic conditions.
  • To elucidate the effects of osmolytes and salts on protein conformation and mobility.

Main Methods:

  • Free boundary capillary electrophoresis was employed to study ferricytochrome c.
  • Mobility measurements were analyzed in the presence of glucitol (sorbitol) and neutral salts.

Main Results:

  • Glucitol (sorbitol) addition shifted the equilibrium towards the molten globule, decreasing mobility due to viscosity.
  • Neutral salts also decreased mobility, primarily due to electrostatic screening.
  • Anion binding, not just screening, influences conformational shifts for some salts.

Conclusions:

  • Both extended coil and molten globule conformations of cytochrome c are free-draining during electrophoresis.
  • Preferential anion binding plays a significant role in ferricytochrome c conformational transitions in acidic media.

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