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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Amyloid Fibrils03:03

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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.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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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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Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
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Protein Folding01:25

Protein Folding

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

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Protein aggregates: Forms, functions and applications.

Joyeeta Mukherjee1, Munishwar Nath Gupta1

  • 1Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology Delhi, Hauz Khas, New Delhi 110016, India.

International Journal of Biological Macromolecules
|November 10, 2016
PubMed
Summary

Catalytically active protein aggregates, including inclusion bodies and amyloids, are increasingly utilized in biocatalysis and food processing. This review explores their characterization techniques.

Keywords:
CaseinsCrosslinked enzyme aggregates (CLEAs)Enzymes in detergentsFood proteinsInclusion bodiesIntrinsically disordered proteinsMembrane proteinsThree phase partitioning of proteins

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Area of Science:

  • Biochemistry
  • Biotechnology

Background:

  • Protein aggregation, including inclusion bodies and amyloids, is a significant biochemical phenomenon.
  • Recent findings highlight the catalytic activity of enzyme inclusion bodies.
  • Protein aggregates have practical applications in various industries.

Purpose of the Study:

  • To review the catalytic activity and applications of protein aggregates.
  • To discuss the role of protein aggregates in biocatalysis, food processing, and detergents.
  • To cover techniques for characterizing protein aggregates.

Main Methods:

  • Literature review of scientific publications on protein aggregation and its applications.
  • Analysis of studies on enzyme inclusion bodies and their catalytic properties.
  • Compilation of information on characterization methods for protein aggregates.

Main Results:

  • Enzyme inclusion bodies are catalytically active and useful in biocatalysis.
  • Protein aggregates find applications in processed foods and as components in detergent granulates.
  • Various techniques exist for characterizing the structure and function of protein aggregates.

Conclusions:

  • Protein aggregates, particularly catalytically active enzyme inclusion bodies, offer significant potential in industrial applications.
  • Understanding and characterizing protein aggregates is crucial for optimizing their use in biocatalysis and other fields.
  • Further research into protein aggregate characterization will enhance their utility.