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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.
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

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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.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...

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The Unfolded Protein Response

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Cotranslational Protein Translocation

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
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Related Experiment Video

Updated: Jun 3, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

A function for the prion protein?

D R Brown¹, I M Jones

¹Department of Biochemistry, University of Cambridge, Cambridge, UK.

Methods in Molecular Medicine

|March 5, 2011

Summary

Prion proteins, linked to spongiform encephalopathies, lacked a clear function until their association with a host gene. Research now explores their role in disease pathogenesis and normal function.

Area of Science:

Neuroscience
Molecular Biology
Genetics

Background:

Prion proteins (PrP) are associated with spongiform encephalopathies.
Their specific physiological function remained elusive until recent investigations.
The infectious agent, PrPSc, was linked to the normal host gene locus, prnp.

Purpose of the Study:

To investigate the function of prion proteins.
To understand the relationship between prion protein function and disease phenotype.
To explore the implications of prion gene identification and sequencing.

Main Methods:

Characterization of the infectious prion agent.
Identification and sequencing of the prion gene (prnp) in mice and humans.
Analysis of protein translation and sequence homology.

More Related Videos

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain

Published on: October 3, 2012

Purification of Hsp104, a Protein Disaggregase

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

Related Experiment Videos

Last Updated: Jun 3, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain

Published on: October 3, 2012

Purification of Hsp104, a Protein Disaggregase

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

Main Results:

The prion gene (prnp) was identified on mouse chromosome 2 and human chromosome 20.
Sequencing of the prnp gene allowed for protein translation and functional speculation.
Established a link between the infectious agent (PrPSc) and the host gene (prnp).

Conclusions:

The identification and sequencing of the prion gene have opened avenues for understanding prion protein function.
Further research is needed to fully elucidate the role of prion proteins in both disease and normal physiology.