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Related Concept Videos

Protein Folding01:25

Protein Folding

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
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Amyloid Fibrils03:03

Amyloid Fibrils

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, normally used to...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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.
The...

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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Self-templated nucleation in peptide and protein aggregation.

Stefan Auer1, Christopher M Dobson, Michele Vendruscolo

  • 1Centre for Self Organising Molecular Systems, University of Leeds, Leeds LS2 9JT, United Kingdom. s.auer@leeds.ac.uk

Physical Review Letters
|December 31, 2008
PubMed
Summary

Protein self-assembly into fibrils is key to neurodegenerative diseases. This study reveals a self-templated nucleation mechanism where disordered oligomers reorder into stable fibrillar structures, offering new insights into disease pathways.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Proteins and peptides commonly form ordered fibrillar aggregates.
  • This aggregation process is often nucleation-dependent and involves intermediate oligomeric assemblies.
  • Disordered oligomeric aggregates are linked to neurodegenerative diseases like Alzheimer's and Parkinson's.

Purpose of the Study:

  • To elucidate the self-templated nucleation mechanism governing the transition from disordered oligomers to ordered fibrillar structures.
  • To understand the molecular basis of how polypeptide chains reorder within oligomers.

Main Methods:

  • The study describes a self-templated nucleation mechanism.
  • It focuses on the molecular-level transition between disordered and ordered assemblies.

Main Results:

  • A novel self-templated nucleation mechanism was identified.
  • Polypeptide chains can reorder within oligomers into fibrillar structures.
  • The surfaces of fibrillar assemblies act as templates, stabilizing disordered oligomers.

Conclusions:

  • The findings provide a molecular understanding of protein self-assembly.
  • This mechanism explains the transition from disordered to ordered aggregates.
  • Insights into protein misfolding relevant to neurodegenerative diseases are offered.