Related Experiment Video

Updated: Aug 23, 2025

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
06:27

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

9.3K

The residual structure of acid-denatured β2 -microglobulin is relevant to an ordered fibril morphology

Ryosuke Tomiyama1, Masatomo So2,3, Keiichi Yamaguchi4

  • 1Graduate School of Biology-oriented Science and Technology, Kindai University, Wakayama, Japan.

Protein Science : a Publication of the Protein Society
|November 2, 2022
PubMed

Insights

The disulfide bond in beta2-microglobulin (β2m) influences its structure, affecting amyloid fibril formation. Oxidized β2m shows more residual structure, leading to ordered fibrils, while reduced β2m forms less ordered fibrils.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Beta2-microglobulin (β2m) forms amyloid fibrils under acidic conditions.
  • Residual structure in acid-denatured β2m influences fibril seeding and extension.
  • Disulfide bond status (oxidized vs. reduced) impacts β2m fibril morphology.

Purpose of the Study:

  • To clarify how the disulfide bond in β2m affects its residual structure and subsequent fibril formation.
  • To investigate the role of residual structure in acid-denatured β2m conformations relevant to amyloid assembly.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was employed to study β2m structure.
  • Comparison of oxidized and reduced β2m under acidic conditions.

Main Results:

  • Oxidized β2m exhibits residual structure throughout the molecule, including termini.
  • Reduced β2m shows localized residual structure with random coil regions.
  • The extent of residual structure in oxidized β2m is broader than the fibril core.
  • Acid-denatured β2m exists in variable conformations, with most not participating in fibril formation due to hidden core residues.

Conclusions:

  • The disulfide bond significantly influences the residual structure of acid-denatured β2m.
  • Conformational selection, where hydrophobic residues become exposed, is crucial for ordered amyloid fibril assembly.
  • Variable conformations of β2m contribute to the complexity of amyloid formation pathways.
Keywords:
NMRamyloid fibrildenatured statehigh-pressure experimentmorphologyresidual structureβ2-microglobulin

More Related Videos

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy14:55

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

Published on: September 17, 2017

15.5K
Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

15.5K

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,...
9.7K
Protein Folding01:22

Protein Folding

Overview
119.1K
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
80.3K
Protein Organization01:13

Protein Organization

Overview
139.7K
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
44.0K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
18.2K