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Related Concept Videos

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can...
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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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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 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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Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
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Repurposing proteins for new bioinorganic functions.

Lewis A Churchfield1, Athira George1, F Akif Tezcan2

  • 1Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0356, U.S.A.

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Scientists are engineering novel metalloproteins with unique properties beyond natural evolution. This research explores new bioinorganic chemistry applications in synthetic biology, biotechnology, and materials science.

Keywords:
biocatalysisbiomaterialsdirected evolutionprotein engineeringstructural biology

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Area of Science:

  • Bioinorganic Chemistry
  • Protein Engineering
  • Synthetic Biology

Background:

  • Natural metalloproteins showcase complex metal-protein interactions.
  • Traditional protein design focuses on mimicking evolutionary principles.
  • Recent advances enable the creation of artificial metalloproteins.

Purpose of the Study:

  • Highlight novel metalloprotein engineering efforts.
  • Showcase properties transcending evolutionary limits.
  • Connect bioinorganic chemistry with emerging fields.

Main Methods:

  • Review of recent advancements in protein design.
  • Exploration of synthetic biology and supramolecular chemistry integration.
  • Discussion of materials engineering applications.

Main Results:

  • Demonstration of engineered metalloproteins with novel functions.
  • Examples of properties exceeding natural evolutionary boundaries.
  • Identification of new interdisciplinary research avenues.

Conclusions:

  • Protein engineering can create metalloproteins with unprecedented properties.
  • Bioinorganic chemistry is expanding into synthetic biology and materials science.
  • This field offers significant potential for biotechnology and beyond.