Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Cooperative structural transitions in amyloid-like aggregation.

Timothy Steckmann1, Yuba R Bhandari1, Prem P Chapagain1

  • 1Department of Physics, Florida International University, Miami, Florida 33199, USA.

The Journal of Chemical Physics
|April 10, 2017
PubMed
Summary

Molecular dynamics simulations reveal a specific temperature window critical for amyloid protofibril formation in the ccβ protein. This finding sheds light on the structural transitions underlying amyloid diseases like Alzheimer's.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

SPNS2 exports sphingosine-1-phosphate and imports glucose.

Nature communications·2026
Same author

Mapping Native Peptide-Peptide Noncovalent Interactions: Insights from Trapped Ion Mobility Spectrometry, Electron- and UV-Fragmentation, Tandem Mass Spectrometry, and Molecular Dynamics.

Journal of the American Society for Mass Spectrometry·2026
Same author

Lasso Peptide Syanodin I: Loop-Pulling Two-Step Thermal Unthreading Mechanism.

Analytical chemistry·2025
Same author

Variants of the Ebola virus matrix protein VP40 have differential effects on oligomerization and plasma membrane interactions.

The Journal of biological chemistry·2025
Same author

Mapping the Interactions Among Class IIa Histone Deacetylases and Myocyte Enhancer Factor 2s.

Journal of chemical information and modeling·2025
Same author

Design of a stapled peptide that binds to the Ebola virus matrix protein dimer interface.

RSC chemical biology·2025

Area of Science:

  • Biochemistry
  • Computational Biology
  • Structural Biology

Background:

  • Amyloid fibril aggregation is linked to neurodegenerative diseases, including Alzheimer's and Parkinson's.
  • These fibril formations share a common cross-β structural motif, despite diverse protein origins.
  • Amyloid formation involves complex pathways with various intermediate aggregates.

Purpose of the Study:

  • To investigate the molecular mechanisms of protein structural transitions during amyloid aggregation.
  • To utilize molecular dynamics (MD) simulations on the model protein ccβ to understand protofibril formation.
  • To explore the thermodynamics and cooperativity of these structural transformations.

Main Methods:

  • Employed molecular dynamics (MD) simulations to study amyloid protofibril formation in the ccβ protein.

Related Experiment Videos

  • Analyzed hydrogen bond dynamics, including the breaking of intrachain bonds and formation of interchain bonds.
  • Investigated the temperature dependence of structural transitions during aggregation.

    • Main Results:

    • Identified two key hydrogen bond transition processes involved in fibril aggregation.
    • Observed a distinct temperature window influencing ccβ protein's protofibril formation.
    • Characterized the thermodynamics and cooperativity of the observed structural transformations.

    Conclusions:

    • The temperature dependence of structural transitions in ccβ suggests a critical window for protofibril formation.
    • Similar temperature-dependent or biochemically controlled transitions may occur in other amyloid-forming proteins.
    • Understanding these molecular dynamics is crucial for insights into amyloid-related diseases.