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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • High concentrations of macromolecules in cells impact protein and protein complex stability.
  • Both physical (hard repulsions) and chemical interactions contribute to this effect.
  • Chemical interactions' role in intracellular protein stability remains understudied.

Purpose of the Study:

  • To investigate the impact of the intracellular environment on protein structure.
  • To characterize the domain-swapped dimer of the B1 domain of protein G in vitro and in vivo.
  • To elucidate the role of chemical interactions versus hard repulsions in cellular protein stability.

Main Methods:

  • Heteronuclear, multidimensional nuclear magnetic resonance (NMR) spectroscopy was employed.
  • Protein G's B1 domain was studied in both buffer solutions and within Escherichia coli cells.
  • Urea was used to probe protein unfolding mechanisms.

Main Results:

  • In buffer, the B1 domain monomer exists as a partially folded molten globule.
  • This molten globule species was not observed in Escherichia coli cells.
  • Urea experiments indicated the monomer is unfolded in cells, lacking the molten-globule form.
  • Attractive chemical interactions in the cytoplasm appear to drive the unfolding of the molten globule.

Conclusions:

  • The intracellular environment significantly modulates protein complex stability.
  • The cellular milieu can alter the predominant species of proteins present.
  • Chemical interactions are likely more critical than hard repulsions for protein behavior within cells.