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Quantifying and visualizing weak interactions between anions and proteins.

Binhan Yu1, Channing C Pletka1, Junji Iwahara2

  • 1Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555-1068.

Proceedings of the National Academy of Sciences of the United States of America
|December 29, 2020
PubMed
Summary
This summary is machine-generated.

This study reveals how anions interact with proteins using NMR spectroscopy. Anions rapidly diffuse around charged proteins and are released upon protein-DNA complex formation, offering insights into electrostatic interactions.

Keywords:
dynamicselectrostatic interactionsionsnuclear magnetic resonanceproteins

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Area of Science:

  • Biochemistry
  • Biophysics
  • Molecular Biology

Background:

  • Protein molecular properties are influenced by solution ions.
  • Weakly interacting ion-protein behaviors are not well understood, unlike strong multivalent ion interactions.

Purpose of the Study:

  • Investigate anion-protein interactions for proteins of similar size but differing charges.
  • Quantify anion accumulation around proteins using a novel NMR approach.
  • Characterize anion dynamics and spatial distribution, especially during protein-DNA complex formation.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to quantify anion accumulation.
  • Poisson-Boltzmann theory for theoretical comparison.
  • Paramagnetic Relaxation Enhancement (PRE) to visualize anion spatial distribution.
  • Measurement of ionic diffusion rates.

Main Results:

  • Anion accumulation around proteins was less than predicted by overall charge valence, aligning with Poisson-Boltzmann theory.
  • NMR revealed rapid diffusion of anions bound to positively charged proteins.
  • Anion release from protein surfaces was observed upon Antp homeodomain-DNA complex formation.
  • PRE data confirmed anion localization near charged protein regions and their release during complexation.

Conclusions:

  • The study elucidates the dynamic behavior of electrostatically interacting anions with proteins.
  • NMR and PRE provide powerful tools for studying weak ion-protein interactions.
  • Anion release upon protein-DNA association highlights the dynamic nature of these interactions.