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Related Concept Videos

Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Protein Folding01:22

Protein Folding

Overview
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...
Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
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...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...

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Related Experiment Video

Updated: May 16, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
08:53

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

Published on: March 21, 2025

C-terminal turn stability determines assembly differences between Aβ40 and Aβ42.

Robin Roychaudhuri1, Mingfeng Yang, Atul Deshpande

  • 1Department of Neurology, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA.

Journal of Molecular Biology
|November 17, 2012
PubMed
Summary
This summary is machine-generated.

A specific C-terminal turn in amyloid beta-42 (Aβ42) drives its aggregation and toxicity in Alzheimer's disease. This Val36-Gly37 turn, absent in Aβ40, is a potential therapeutic target.

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Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain
09:35

Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain

Published on: October 24, 2017

Related Experiment Videos

Last Updated: May 16, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
08:53

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

Published on: March 21, 2025

Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain
09:35

Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain

Published on: October 24, 2017

Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Amyloid beta-protein (Aβ) oligomerization is central to Alzheimer's disease pathogenesis.
  • Aβ42 is significantly more pathogenic than Aβ40, but the structural basis remains unclear.

Purpose of the Study:

  • To elucidate the structural differences between Aβ42 and Aβ40 that explain their differential pathogenicity.
  • To investigate the role of a specific C-terminal turn in Aβ42 structure and function.

Main Methods:

  • Computational modeling to predict protein structures.
  • Chemical synthesis of modified amyloid beta peptides.
  • Analysis of peptide oligomerization and secondary structure formation.
  • Assessment of the toxicity of different Aβ assemblies.

Main Results:

  • A C-terminal Val36-Gly37 turn and a stabilizing β-hairpin structure were identified in Aβ42, absent in Aβ40.
  • Amino acid substitutions altering this turn modulated Aβ42 oligomerization and toxicity.
  • Introducing the Aβ42-like turn into Aβ40 increased its oligomerization, toxicity, and altered its assembly characteristics.

Conclusions:

  • The Val36-Gly37 turn is a critical structural determinant of Aβ42 pathogenicity.
  • This turn may be the key feature distinguishing Aβ42 from Aβ40.
  • The Aβ42 C-terminal turn represents a promising therapeutic target for Alzheimer's disease.