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Amyloid Fibrils

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 Fibrils

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...

Translation

Translation

Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life

Translation

Translation

Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life

Mutations

Mutations

Mutations

Mutations

Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. Mutations can be characterized in a number of different ways: whether and how they alter the amino acid sequence of the protein, whether they occur over a small or large area of DNA, and whether they occur in somatic cells or germline cells.
Chromosomal Alterations Are Large-Scale Mutations
While point mutations are changes in a single nucleotide in...

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Related Experiment Video

Updated: Jun 29, 2026

Assays for the Degradation of Misfolded Proteins in Cells

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

DE loop mutations affect beta2-microglobulin stability and amyloid aggregation.

Stefano Ricagno¹, Matteo Colombo, Matteo de Rosa

¹Department of Biomolecular Sciences and Biotechnology, CNR-INFM and CIMAINA, University of Milano, Milano, Italy.

Biochemical and Biophysical Research Communications

|October 7, 2008

Summary

This summary is machine-generated.

Beta2-microglobulin (beta2m) aggregation is influenced by its DE loop. Mutations in this loop, particularly at Trp60 and Asp59, alter beta2m stability and amyloid formation propensity, impacting MHC-I assembly.

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Area of Science:

Biochemistry
Structural Biology
Immunology

Background:

Beta2-microglobulin (beta2m) is essential for class I major histocompatibility complex (MHC-I) assembly.
Beta2-microglobulin is an intrinsically amyloidogenic protein, prone to forming amyloid fibrils.
The DE loop of beta2m is implicated in protein stability and amyloid aggregation.

Purpose of the Study:

To investigate the role of the DE loop in beta2m stability and amyloid aggregation.
To analyze the impact of specific mutations (Trp60-->Cys and Asp59-->Pro) on beta2m properties.

Main Methods:

Expression and purification of beta2m mutants (Trp60-->Cys, Asp59-->Pro).
Determination of crystal structures for the mutants.
Analysis of thermal denaturation stability.
Assessment of propensity for fibrillar aggregation.

Main Results:

The crystal structures of Trp60-->Cys and Asp59-->Pro beta2m mutants were determined.
Mutant analysis revealed altered protein stability and aggregation tendencies.
Experimental data support the hypothesis that DE loop conformational strain affects beta2m stability and amyloidogenicity.

Conclusions:

Conformational strain within the beta2m DE loop significantly influences protein stability.
Modifications in the DE loop can modulate the propensity of beta2m to form amyloid aggregates.
Understanding these mechanisms is crucial for diseases associated with beta2m amyloidosis.