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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,...

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In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...

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Related Experiment Video

Updated: Aug 11, 2025

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Solid-state NMR studies of amyloids.

Jing Liu¹, Xia-Lian Wu¹, Yu-Teng Zeng¹

¹School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.

Structure (London, England : 1993)

|February 7, 2023

Summary

This summary is machine-generated.

Solid-state NMR (SSNMR) advances our understanding of amyloid structures and dynamics, crucial for studying neurodegenerative diseases. This review highlights key research and technical developments in the field.

Keywords:

amyloids functional amyloids neurodegenerative diseases phase separation solid-state NMR

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Area of Science:

Biochemistry
Structural Biology
Neuroscience

Background:

Amyloids are implicated in severe neurodegenerative diseases.
Their high molecular weight and aggregation present research challenges.
Solid-state NMR (SSNMR) is a key technique for amyloid studies.

Purpose of the Study:

To review the application of SSNMR in amyloid research.
To highlight progress in understanding amyloid structures and dynamics.
To showcase technical advancements in SSNMR for biological studies.

Main Methods:

Extensive application of solid-state NMR (SSNMR) spectroscopy.
Analysis of amyloid structures and dynamics.
Review of relevant research studies and technical developments.

Main Results:

SSNMR has significantly advanced the understanding of amyloid structures and dynamics.
Research on amyloids has driven technical improvements in SSNMR sensitivity and resolution.
A comprehensive overview of current research and technical progress is provided.

Conclusions:

SSNMR is indispensable for elucidating amyloid structures and their role in disease.
Continued technical development of SSNMR will further enhance amyloid research.
This review offers insights into the current state of amyloid and SSNMR studies.