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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...
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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Anomalous Protein-Protein Interactions in Multivalent Salt Solution.

Coralie Pasquier1, Mario Vazdar2, Jan Forsman1

  • 1Division of Theoretical Chemistry, Lund University , POB 124, SE-22100 Lund, Sweden.

The Journal of Physical Chemistry. B
|March 21, 2017
PubMed
Summary
This summary is machine-generated.

Multivalent ions significantly impact protein stability in water. Simulations reveal complex protein-protein interactions, including attraction and repulsion, influenced by electrolyte concentration and ion correlations.

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Area of Science:

  • Physical Chemistry
  • Biophysics
  • Computational Biology

Background:

  • Aqueous protein solution stability is sensitive to multivalent ions.
  • Ion-induced correlations extend beyond classical mean-field theory.

Purpose of the Study:

  • Investigate protein-protein interactions in 3:1 electrolyte solutions.
  • Understand the role of ion-ion correlations in protein behavior.

Main Methods:

  • All-atom molecular dynamics (MD) simulations.
  • Coarse-grained Monte Carlo (MC) simulations.
  • Hybrid continuum solvent models for efficient sampling.

Main Results:

  • Observed anomalous protein-protein potential of mean force with increasing electrolyte concentration.
  • Identified distinct interaction regimes: repulsion, attraction, overcharge repulsion, and non-Coulombic attraction.
  • Validated findings against experimental 'reentrant protein condensation' observations.

Conclusions:

  • Multivalent ions induce complex, non-mean-field interactions between proteins.
  • Simulations accurately capture experimentally observed phenomena like reentrant condensation.
  • Hybrid models offer efficient approaches for studying large-scale protein-ion systems.