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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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Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor
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Multifunctional Protein Materials and Microreactors using Low Complexity Domains as Molecular Adhesives.

Lenka Faltova, Andreas M Küffner, Maria Hondele

    ACS Nano
    |September 15, 2018
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    Researchers engineered protein-based molecular adhesives using disordered amino acid sequences. These adhesives control protein self-assembly into functional supramolecular architectures, creating novel biomaterials and bioreactors.

    Keywords:
    intrinsically disordered proteinsliquid−liquid phase separationlow complexity domainsmembraneless compartmentsmicroreactorsprotein materialsprotein self-assembly

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    Area of Science:

    • Biochemistry
    • Materials Science
    • Biotechnology

    Background:

    • Disordered amino acid sequences, specifically low complexity domains (LCDs), are known to promote functional phase transitions in biomolecules.
    • These LCDs are rich in specific amino acids and influence biomolecular interactions.

    Purpose of the Study:

    • To develop novel molecular adhesives by conjugating LCDs to soluble globular proteins.
    • To enable sensitive and controlled self-assembly of proteins into functional supramolecular architectures.

    Main Methods:

    • Conjugation of low complexity regions (LCDs) to soluble globular domains (adenylate kinase, green fluorescent protein).
    • Induction of protein particle formation via liquid-liquid phase transition and subsequent maturation into aggregates.
    • Characterization of noncovalent intermolecular interactions and phase properties dictated by LCDs.

    Main Results:

    • Addition of LCDs induced a multistep self-assembly process, starting with liquid-liquid phase separation into protein-rich droplets.
    • These droplets matured into permeable protein aggregates that retained enzymatic activity and released soluble proteins.
    • LCDs determined phase properties largely independent of the attached globular domain.

    Conclusions:

    • Engineered protein-based molecular adhesives can precisely control protein self-assembly into higher-order structures.
    • The developed system allows for the creation of static multifunctional biomaterials and dynamic microscale bioreactors.
    • This approach offers a versatile platform for designing novel protein-based nanomaterials with tailored functions.