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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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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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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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Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Ligand Binding and Linkage00:49

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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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Protein-protein Interfaces

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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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Intrinsically Disordered Proteins

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Programming interchangeable and reversible heterooligomeric protein self-assembly using a bifunctional ligand.

Soyeun Son1, Woon Ju Song1

  • 1Department of Chemistry, College of Natural Sciences, Seoul National University Seoul 08826 Republic of Korea woonjusong@snu.ac.kr.

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|February 26, 2024
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Researchers developed a versatile bifunctional linker to create tunable protein heterooligomers for biomaterials. This method enables modular assembly of diverse protein components, expanding possibilities for novel functional architectures.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Synthetic Biology

Background:

  • Protein self-assembly is crucial for understanding biological structures and designing novel biomaterials.
  • Heterooligomers offer greater structural and functional diversity compared to homooligomers.
  • Interchangeable protein components could significantly expand the repertoire of macromolecular applications.

Purpose of the Study:

  • To demonstrate a method for creating diverse protein heterooligomers using a rationally designed bifunctional linker.
  • To show that this approach allows for easily applicable and exchangeable protein components without extensive sequence optimization.
  • To explore the tunability and reversibility of protein self-assembly guided by the linker.

Main Methods:

  • Design of a bifunctional linker incorporating an enzyme inhibitor and a maleimide group.
  • Selection of four structurally and functionally distinct proteins (carbonic anhydrase, aldolase, acetyltransferase, encapsulin) as building blocks.
  • Assembly of two-component heterooligomers using the bifunctional linker and characterization of their properties.

Main Results:

  • Successfully formed four distinct two-component heterooligomers with varied sizes, shapes, and enzymatic activities.
  • Demonstrated that heterooligomer formation kinetics and size are tunable by external stimuli like metal chelators, acidic buffers, and reducing agents.
  • Confirmed the reversibility and modularity of the protein self-assembly process.

Conclusions:

  • The developed bifunctional linker enables the rational design and construction of diverse, tunable protein heterooligomers.
  • This modular approach broadens the scope of protein-assembled architectures for potential applications as functional biomaterials.
  • The interchangeability of linker and protein components offers a flexible platform for advanced biomaterial development.