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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. 
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Protein Folding01:25

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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.
Protein Structure Is Critical to Its Biological Function
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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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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Protein aggregation: An overview.

Bahareh Dabirmanesh1, Khosro Khajeh1, Vladimir N Uversky2

  • 1Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.

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Protein misfolding and aggregation into amyloid structures can disrupt cellular processes and contribute to aging and neurodegenerative diseases. However, some amyloids also have crucial physiological roles, highlighting the complexity of protein aggregation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Proteins require specific molecular structures for function, encoded in their amino acid sequences.
  • Protein folding is essential for achieving a unique functional state.
  • Misfolding and aggregation can lead to detrimental structures like amyloid aggregates with cross-β structure.

Purpose of the Study:

  • To provide an overview of protein aggregation.
  • To outline key discoveries in the field of protein aggregation.
  • To discuss the dual role of amyloids in pathology and physiology.

Main Methods:

  • Literature review of protein folding and aggregation.
  • Historical timeline of key discoveries in protein aggregation research.
  • Analysis of the impact of protein aggregates on cellular processes.

Main Results:

  • Protein aggregates, particularly amyloid structures, can disrupt proteostasis.
  • Imbalances in proteostasis contribute to aging and neurodegenerative diseases.
  • Functional amyloids play essential roles in various biological processes.

Conclusions:

  • Protein aggregation is a complex phenomenon with both pathological and physiological implications.
  • Understanding protein aggregation is crucial for addressing age-related diseases.
  • The field of protein aggregation has a rich history of significant discoveries.