Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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...

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

Protein Folding

Protein Folding

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

Actin Polymerization

Actin Polymerization

Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶ nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight actin...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Targeting the METTL1/m7G axis as a therapeutic strategy in myeloid leukemia.

Blood·2026

Same author

Unusual backfolded binding poses of BAZ2A bromodomain binders.

Acta crystallographica. Section D, Structural biology·2026

Same author

Ligand-Induced Opening of a Cryptic Pocket in METTL14.

ACS bio & med chem Au·2026

Same author

Fine-Tuning a Transformer Model for METTL3 Lead Optimization.

ACS bio & med chem Au·2026

Same author

Indirect inhibition of the NLRP3-interleukin-1β axis contributes to the efficacy of JAK1 inhibitors in experimental colitis and human ulcerative colitis.

Nature communications·2026

Same author

Antigen-directed single domain antibody-based TNFR1 agonists elicit preferential killing of HER2-overexpressing cancer cells.

iScience·2026

Search research articles

Related Experiment Video

Updated: Jun 8, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

Amyloid fibril polymorphism is under kinetic control.

Riccardo Pellarin¹, Philipp Schuetz, Enrico Guarnera

¹Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.

Journal of the American Chemical Society

|October 7, 2010

Summary

Amyloid aggregates exhibit diverse structures. This study reveals that less stable fibril shapes often form first, indicating that the speed of formation, not just stability, dictates amyloid polymorphism.

More Related Videos

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

Related Experiment Videos

Last Updated: Jun 8, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

Area of Science:

Biochemistry
Biophysics
Computational Biology

Background:

Protein self-assembly into amyloid fibrils is implicated in various diseases.
Amyloid formation exhibits significant morphological diversity (polymorphism).
Factors governing the equilibrium of distinct fibril morphologies remain unclear.

Purpose of the Study:

To investigate the nucleation pathways of distinct amyloid fibril morphologies.
To determine the influence of external conditions on amyloid polymorphism.
To elucidate the kinetic versus thermodynamic control of fibril formation.

Main Methods:

Utilized computer simulations of a simplified amyloid polypeptide model.
Analyzed free-energy profiles of the protein aggregation process.
Investigated nucleation barriers for different fibril morphologies.

Main Results:

Counterintuitively, less energetically favorable fibril morphologies nucleated more frequently.
This phenomenon was observed in models with low aggregation propensity.
Nucleation barriers were identified as key determinants of fibril morphology populations.

Conclusions:

Amyloid polymorphism is primarily under kinetic control, not thermodynamic equilibrium.
The nucleation barrier significantly influences the relative abundance of different fibril structures.
Understanding these kinetic factors is crucial for controlling amyloid self-assembly.