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Related Experiment Videos

Anion binding to the ubiquitin molecule

G I Makhatadze1, M M Lopez, J M Richardson

  • 1Department of Chemistry and Biochemistry, Texas Tech University, Lubbock 79409-1061, USA. gia@ttu.edu

Protein Science : a Publication of the Protein Society
|April 16, 1998
PubMed
Summary

Different salts enhance ubiquitin molecule stability at pH 2.0 by binding anions, with chloride ions showing weak binding and negative enthalpy. Guanidinium chloride also stabilizes ubiquitin, likely due to chloride ion interactions.

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Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Molecular Biology

Background:

  • Ubiquitin is a crucial protein involved in various cellular processes.
  • Protein stability is influenced by environmental factors, including salt concentrations.
  • Understanding protein-salt interactions is key to comprehending protein function and behavior.

Purpose of the Study:

  • To investigate the effects of various salts on the stability of ubiquitin at low pH.
  • To elucidate the mechanisms underlying salt-induced stabilization of ubiquitin.
  • To quantify the thermodynamic parameters of anion binding to ubiquitin.

Main Methods:

  • Differential scanning calorimetry (DSC) to measure thermal stability.
  • Circular dichroism (CD) spectroscopy to assess protein structure.

Related Experiment Videos

  • Tyrosine (Tyr) fluorescence spectroscopy to probe protein conformational changes.

    • Main Results:

    • All tested salts (NaCl, MgCl2, CaCl2, GdmCl, NaBr, NaClO4, NaH2PO4, Na2SO4) increased ubiquitin's thermostability at pH 2.0.
    • Stabilization was attributed to anion binding, with chloride ions exhibiting weak binding (Kd = 0.15 M) and a negative enthalpy (-15 kJ/mol per site).
    • Guanidinium chloride (GdmCl) demonstrated a concentration-dependent stabilizing effect, attributed to chloride ion binding.

    Conclusions:

    • Anions play a significant role in stabilizing the ubiquitin molecule at acidic pH.
    • The binding of chloride ions to ubiquitin is characterized by weak affinity and favorable enthalpy.
    • GdmCl's stabilizing effect is primarily driven by its associated chloride ions, highlighting the complex interplay of denaturants and ions in protein stability.