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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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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.
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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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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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What are Proteins?

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Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight.  Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional...
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Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
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OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
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Programmable polyproteams built using twin peptide superglues.

Gianluca Veggiani1, Tomohiko Nakamura2, Michael D Brenner1

  • 1Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, United Kingdom;

Proceedings of the National Academy of Sciences of the United States of America
|January 21, 2016
PubMed
Summary
This summary is machine-generated.

Researchers created programmable protein chains called polyproteins using novel SnoopTag and SpyTag systems. This breakthrough allows precise assembly of protein units for advanced biological applications and cancer research.

Keywords:
antibodynanobiotechnologyprotein engineeringsplit proteinsynthetic biology

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Synthetic Biology

Background:

  • Protein engineering is complex due to multiple reactive groups and stability issues.
  • Previous methods lacked precise control over protein assembly.
  • Amino acid and nucleotide chain programming revolutionized biological control.

Purpose of the Study:

  • To develop a method for sequence-programmed, irreversible connection of protein units.
  • To create programmable protein chains (polyproteins) with modularity and precision.
  • To explore applications in cancer cell death signal activation.

Main Methods:

  • Engineered SnoopTag peptide and SnoopCatcher protein, forming a spontaneous isopeptide bond with high yield and specificity.
  • Utilized SpyTag/SpyCatcher system alongside the new SnoopTag/SnoopCatcher system.
  • Employed solid-phase attachment and sequential tagging for iterative protein extension.

Main Results:

  • Successfully synthesized linear, branched, and combinatorial polyproteins.
  • Achieved >99% yield and no cross-reactivity with the SnoopTag/SnoopCatcher system.
  • Identified optimal ligand combinations for activating cancer cell death signals.

Conclusions:

  • Developed a simple, modular route to programmable polyproteins ('polyproteams').
  • This method enables precise control over protein assembly for diverse biological functions.
  • Opens new avenues for exploring biological space and therapeutic development.