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Related Experiment Videos

Dimer formation by a "monomeric" protein.

C Park1, R T Raines

  • 1Department of Biochemistry, University of Wisconsin-Madison, 53706, USA.

Protein Science : a Publication of the Protein Society
|December 6, 2000
PubMed
Summary
This summary is machine-generated.

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Ribonuclease A (RNase A) can form active dimers, challenging its monomer assumption. This protein dimerization occurs under physiological conditions, suggesting dimers may be common in biology.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Structure

Background:

  • Dimeric proteins can form through domain swapping between monomers.
  • Ribonuclease A (RNase A) is typically considered a monomer under physiological conditions.
  • The prevalence of domain swapping in protein dimerization is not well understood.

Purpose of the Study:

  • To investigate the dimerization of Ribonuclease A (RNase A) under physiological conditions.
  • To determine if RNase A can form active dimers in vivo.
  • To assess the prevalence of dimeric forms of proteins typically considered monomers.

Main Methods:

  • Site-directed mutagenesis to create H12A and H119A RNase A variants.
  • Enzyme activity assays to measure ribonucleolytic activity.

Related Experiment Videos

  • Incubation and lyophilization techniques to promote dimer formation.
  • Determination of equilibrium dissociation constants (Kd) for dimer formation.

    • Main Results:

    • H12A and H119A RNase A variants exhibit significantly reduced activity compared to wild-type.
    • Mixing and incubating H12A and H119A variants restores significant ribonucleolytic activity, forming active dimers.
    • Active RNase A dimers can be efficiently produced via lyophilization.
    • The equilibrium dissociation constant (Kd) for RNase A dimer formation is approximately 2 mM, suggesting in vivo dimerization.

    Conclusions:

    • RNase A possesses an intrinsic ability to form dimers under physiological conditions.
    • The formation of RNase A dimers in vivo is plausible given the observed Kd and physiological concentrations.
    • Dimeric forms of proteins commonly regarded as monomers may be more widespread than previously recognized.