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Intracellular pH modulates quinary structure.

Rachel D Cohen1, Alex J Guseman1, Gary J Pielak1,2,3

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

Protein Science : a Publication of the Protein Society
|August 11, 2015
PubMed
Summary
This summary is machine-generated.

Intracellular pH affects protein interactions within cells. Changes in pH alter these interactions, impacting the quality of NMR spectroscopy data for proteins in vivo.

Keywords:
amide proton exchangein-cell NMRmacromolecular crowdingpHprotein stabilityquinary interactions

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Area of Science:

  • Biochemistry
  • Biophysics
  • Cell Biology

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy provides insights into protein behavior within living cells.
  • Intracellular pH is a critical factor influencing protein properties like charge and stability.
  • Quinary interactions, transient associations between proteins and other macromolecules, are ubiquitous in the cellular environment.

Purpose of the Study:

  • To investigate the influence of intracellular pH on quinary interactions.
  • To determine how pH-modulated quinary interactions affect the quality of in-cell NMR spectra.
  • To utilize a pH-sensitive protein reporter for in-cell studies.

Main Methods:

  • Employing Nuclear Magnetic Resonance (NMR) spectroscopy, specifically in-cell (15)N-(1)H HSQC.
  • Using the K10H variant of the B domain of protein G (GB1) as a pH reporter in Escherichia coli.
  • Manipulating and controlling intracellular pH within the bacterial cells.

Main Results:

  • Intracellular pH significantly modulates quinary interactions.
  • At lower pH, increased attractive interactions between cellular proteins and GB1 were observed.
  • These interactions led to slower GB1 tumbling and broadened NMR crosspeaks, degrading spectral quality.

Conclusions:

  • Quinary interactions are sensitive to intracellular pH.
  • pH-dependent quinary interactions directly impact the quality of in-cell NMR data.
  • Understanding quinary interactions is crucial for interpreting protein behavior in cellular contexts.