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Protein shape modulates crowding effects.

Alex J Guseman1, Gerardo M Perez Goncalves1, Shannon L Speer1

  • 1Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.

Proceedings of the National Academy of Sciences of the United States of America
|October 11, 2018
PubMed
Summary
This summary is machine-generated.

Cellular protein interactions differ from dilute solutions due to high macromolecule concentrations. Protein dimer shape influences hard-core repulsions, affecting protein-protein interactions and cellular regulation.

Keywords:
macromolecular crowdingprotein−protein interactionsscaled particle theory

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Area of Science:

  • Biochemistry
  • Biophysics
  • Molecular Biology

Background:

  • Cellular environments have high macromolecule concentrations (>300 g/L), leading to nonspecific protein-protein interactions.
  • These interactions include hard-core steric repulsions and soft chemical interactions.
  • Scaled particle theory suggests shape influences these interactions.

Purpose of the Study:

  • To test if protein dimer shape affects stabilization by hard-core repulsions.
  • To differentiate the effects of hard-core repulsions versus chemical interactions on protein dimers.

Main Methods:

  • Studied two variants of the B1 domain of protein G, a dumbbell-shaped dimer and an ellipsoidal domain-swapped dimer.
  • Used inert crowding agents (Ficoll, PEG) to simulate hard-core repulsions.
  • Used protein cosolutes to investigate chemical interactions.

Main Results:

  • Hard-core repulsions significantly stabilized the ellipsoidal dimer but had minimal effect on the dumbbell dimer.
  • Protein cosolutes showed similar small effects on both dimer shapes.
  • Results support the hypothesis that dimer shape dictates the impact of hard-core repulsions.

Conclusions:

  • Protein dimer shape is a key factor in how hard-core repulsions influence protein-protein interactions.
  • Cells may utilize dimer shape to regulate interactions in crowded environments.
  • This provides a mechanism for controlling protein complex formation in vivo.