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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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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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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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Protein and Protein Structure02:15

Protein and Protein Structure

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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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Updated: Aug 31, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
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Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

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What makes functional amyloids work?

Ansgar B Siemer1

  • 1Department of Physiology and Neuroscience, Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, Los Angeles, CA, USA.

Critical Reviews in Biochemistry and Molecular Biology
|August 23, 2022
PubMed
Summary
This summary is machine-generated.

Cross-beta (amyloid) fibrils, initially disease-associated, are functional in all life. This review explores their periodic, stable, and self-templating properties that enable biological functions.

Keywords:
Functional amyloidcross-β motifprotein aggregationprotein fibrilsstructure–function relationship

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Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Cross-beta (amyloid) fibrils were first identified in disease contexts.
  • These fibrillar structures are now recognized as functional components across all kingdoms of life.

Purpose of the Study:

  • To elucidate the specific properties of the cross-beta fibril motif that confer biological function.
  • To understand how these properties distinguish functional fibrils from other biological fibrils.

Main Methods:

  • Review and synthesis of existing literature on cross-beta fibril structure and function.
  • Analysis of the inherent properties of the cross-beta fibril structure, including periodicity, stability, and self-templating capabilities.
  • Examination of case studies highlighting functional cross-beta fibrils and their mechanisms.

Main Results:

  • Cross-beta fibrils are characterized by high periodicity, stability, and self-templating formation.
  • Fibril formation involves significant conformational changes, leading to multimerization of core and framing sequences.
  • Biological functions are typically achieved by exploiting multiple properties of the cross-beta fibril structure.

Conclusions:

  • The unique structural properties of cross-beta fibrils (periodicity, stability, self-templating) are key to their diverse biological functions.
  • Understanding these properties provides insight into the evolution and adaptability of fibrillar structures in nature.
  • Functional roles of cross-beta fibrils are diverse and depend on the specific interplay of their inherent structural characteristics.