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Related Concept Videos

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...
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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Protein-protein Interfaces02:04

Protein-protein Interfaces

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 polypeptide...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Mutations01:39

Mutations

Overview

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Related Experiment Video

Updated: Jun 13, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

A single mutation promotes amyloidogenicity through a highly promiscuous dimer interface.

Francis C Peterson1, Elizabeth M Baden, Barbara A L Owen

  • 1Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI 53226, USA.

Structure (London, England : 1993)
|May 14, 2010
PubMed
Summary
This summary is machine-generated.

The light chain dimer interface in amyloidosis shows flexibility. This structural promiscuity may drive the formation of amyloid fibrils, contributing to disease progression.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Medicine

Background:

  • Light chain amyloidosis is a severe protein misfolding disease.
  • Amyloid fibrils, formed by monoclonal light chains, cause organ damage.
  • Understanding light chain protein structure is crucial for disease mechanisms.

Purpose of the Study:

  • To investigate the structural basis of amyloid fibril formation in light chain amyloidosis.
  • To elucidate the role of dimer interface conformation in amyloidogenic processes.
  • To explore the structural dynamics of light chain proteins using NMR.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was employed.
  • The structures of two specific light chain mutants (AL-09 H87Y and kappaI Y87H) were determined.
  • Solution structures of dimer interfaces were analyzed.

Main Results:

  • The kappaI Y87H mutant displayed an altered dimer interface, rotated 180 degrees from the canonical structure.
  • The AL-09 H87Y mutant adopted a normal dimer interface.
  • Conformational heterogeneity in solution obscured wild-type dimer interface signals.

Conclusions:

  • The light chain dimer interface exhibits significant conformational flexibility.
  • This structural promiscuity may facilitate the formation of intermolecular contacts essential for amyloid fibril assembly.
  • Findings offer insights into the molecular mechanisms underlying light chain amyloidosis pathogenesis.