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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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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Isomerism in Complexes
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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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The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
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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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Supramolecular Synthons in Protein-Ligand Frameworks.

Ronan J Flood1, Niamh M Mockler1, Aurélien Thureau2

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Supramolecular synthons, like sulfonato-calix[8]arene, can guide protein crystallization. This research shows how these units direct the assembly of protein RSL into porous crystalline structures, aiding protein crystal engineering.

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Area of Science:

  • Supramolecular chemistry
  • Crystallography
  • Protein engineering

Background:

  • Supramolecular synthons are key to small molecule crystal engineering.
  • Their role in protein crystallization is less understood.
  • The protein RSL and sulfonato-calix[8]arene serve as a model system.

Purpose of the Study:

  • To investigate if supramolecular synthons can guide protein crystallization.
  • To explore the structural diversity of RSL-calixarene cocrystals.
  • To understand the role of calixarene conformation in protein assembly.

Main Methods:

  • Cocrystallization of protein RSL with sulfonato-calix[8]arene.
  • X-ray diffraction analysis of cocrystals.
  • Site-directed mutagenesis of protein RSL.
  • Small-angle X-ray scattering (SAXS) for solution studies.

Main Results:

  • RSL and sulfonato-calix[8]arene form multiple cocrystalline structures, including porous cubes.
  • Mutations in RSL lead to new cubic assemblies mediated by calixarene trimers.
  • The calixarene's pleated loop conformation is conserved between its salt form and protein cocrystals.
  • Calixarene oligomerization in solution is pH-dependent.

Conclusions:

  • Supramolecular synthons, specifically the calixarene-calixarene unit, direct protein assembly.
  • This principle enables engineering of protein crystals with tunable structures.
  • Potential applications in developing novel protein-based materials and drug delivery systems.