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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
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Physicochemical code for quinary protein interactions in Escherichia coli.

Xin Mu1, Seongil Choi1, Lisa Lang1

  • 1Department of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden.

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|May 25, 2017
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Summary

Cellular protein movement follows simple physical-chemical rules, not just random diffusion. Single mutations can optimize protein interactions, aiding biological control and therapeutic development.

Keywords:
in-cell NMRintracellular diffusionprotein surface properties

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Area of Science:

  • Biophysics
  • Cell Biology
  • Protein Dynamics

Background:

  • Protein navigation within the cell is poorly understood.
  • Cellular environments are crowded with largely non-conserved protein surfaces.
  • The role of selection and biological control in protein search is unclear.

Purpose of the Study:

  • To investigate how proteins move and interact within the cellular interior.
  • To determine if protein motion is governed by physical-chemical principles and subject to evolutionary optimization.

Main Methods:

  • In-cell Nuclear Magnetic Resonance (NMR) spectroscopy was used.
  • The motions of three evolutionarily distinct proteins in Escherichia coli cytoplasm were examined.

Main Results:

  • In-cell protein motions depend on net charge density, surface hydrophobicity, and electric dipole moment.
  • Bacterial proteins move more freely than human proteins, which tend to aggregate.
  • Surface mutations predictably alter protein motion, allowing for tunable behavior.

Conclusions:

  • Cytoplasmic protein diffusion follows predictable physical-chemical rules.
  • Evolution can rapidly optimize protein interactions through single-point mutations.
  • This provides a framework for manipulating protein motion for research and therapeutic applications.