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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...

Protein Organization

Protein Organization

Protein Organization

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.

Protein Organization

Protein Organization

Protein Organization

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.

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Related Experiment Video

Updated: Jun 17, 2026

Purification and Refolding to Amyloid Fibrils of (His)6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli

Purification and Refolding to Amyloid Fibrils of (His)₆-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli

Published on: December 19, 2015

beta-sheet constitution of prion proteins.

Hong-Fang Ji¹, Hong-Yu Zhang

¹Shandong Provincial Research Center for Bioinformatic Engineering and Technique, Center for Advanced Study, Shandong University of Technology, Zibo 255049, PR China. jhf@sdut.edu

Trends in Biochemical Sciences

|January 12, 2010

Summary

Structural details of the scrapie prion protein (PrP(Sc)) are crucial for understanding prion diseases (PDs). This study proposes helix 2 is key to PrP(Sc) beta-sheet formation, potentially explaining why non-mammals lack PDs.

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Purification of Hsp104, a Protein Disaggregase

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

Area of Science:

Neuroscience
Structural Biology
Biochemistry

Background:

Understanding the structure of normal prion protein (PrP(C)) and its pathogenic scrapie isoform (PrP(Sc)) is essential for prion disease (PD) pathogenesis.
While PrP(C) structure is known, PrP(Sc) structural details remain elusive, though beta-sheets are recognized as its core component.
The N-terminus beta-sheet composition is agreed upon, but the C-terminal beta-sheet structure is debated.

Purpose of the Study:

To propose a structural hypothesis for the scrapie prion protein (PrP(Sc)) based on recent dynamics and structural data.
To identify which C-terminal helices are most likely involved in the beta-sheet formation characteristic of PrP(Sc).
To offer a potential explanation for the absence of prion diseases in non-mammalian species.

Main Methods:

Review and evaluation of recent findings on prion protein (PrP) dynamics and structures.
Comparative analysis of potential beta-sheet forming regions within the C-terminus of PrP.
Hypothesis generation based on integrated structural and dynamic evidence.

Main Results:

Accumulated evidence suggests beta-sheets form the fundamental structure of PrP(Sc).
Helix 2 is proposed as the most probable C-terminal region to participate in beta-sheet formation in PrP(Sc).
This hypothesis offers a potential mechanism for the resistance of non-mammals to prion diseases.

Conclusions:

The proposed role of helix 2 in PrP(Sc) beta-sheet formation provides a novel structural insight.
This structural model may elucidate the species barrier observed in prion diseases.
Further research is warranted to experimentally validate the proposed structural model of PrP(Sc).