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Related Concept Videos

Protein Complex Assembly02:41

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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Protein Complexes with Interchangeable Parts01:57

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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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Conservation of Protein Domains Over Different Proteins02:26

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Assembly of Signaling Complexes01:30

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
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Protein-protein Interfaces02:04

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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Cooperative Allosteric Transitions01:58

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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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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

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Heterogeneous protein co-assemblies with tunable functional domain stoichiometry.

Shaheen A Farhadi1, Antonietta Restuccia1, Anthony Sorrentino1

  • 1J. Crayton Pruitt Family Department of Biomedical Engineering, University of Florida, Gainesville, FL, 32611, USA.

Molecular Systems Design & Engineering
|May 2, 2022
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Summary

Scientists engineered novel protein assemblies using a three-stranded coiled-coil scaffold. This method allows precise control over subunit stoichiometry, creating versatile supramolecular machines for diverse applications.

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Area of Science:

  • Biochemistry
  • Synthetic Biology
  • Protein Engineering

Background:

  • Nature utilizes heterogeneous protein co-assembly for complex supramolecular machines.
  • Synthetic approaches can create novel protein machines with enhanced functions.

Purpose of the Study:

  • To develop a synthetic method for creating supramolecular machines with tunable subunit stoichiometry.
  • To demonstrate the modular assembly of proteins using a heterotrimeric coiled-coil scaffold.

Main Methods:

  • Fusion of distinct peptide strands (A, B, C) of a heterotrimeric coiled-coil to different proteins (NanoLuc luciferase, sfGFP, mRuby).
  • Utilizing bioluminescence and fluorescence resonance energy transfer (BRET/FRET) for simultaneous light emission.
  • Incorporating galectin-3 domains to impart tunable lactose-binding affinity.

Main Results:

  • Formation of ternary complexes (NL-A, sfGFP-B, mRuby-C) capable of simultaneous blue, green, and red light emission via BRET/FRET.
  • Demonstrated tunable lactose-binding affinity by varying galectin-3 integration (1-3 domains) while preserving BRET/FRET.
  • Achieved greater control over subunit combinations compared to previous heterodimeric coiled-coil systems.

Conclusions:

  • The modular fusion protein design and coiled-coil scaffold enable precise control over protein co-assembly and stoichiometry.
  • This approach expands the diversity of co-integrated protein domains for designing advanced supramolecular machines.
  • Potential applications in therapeutics, diagnostics, and biotechnology.