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

One-dimensional model of yeast prion aggregation.

K C Kunes1, D L Cox, R R P Singh

  • 1Department of Physics, University of California, Davis, California 95616, USA.

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|December 31, 2005
PubMed
Summary

Yeast prions like SUP35, simpler models for mammalian prion proteins (PrP), exhibit exponential growth and long aggregates. Aggregate fissioning is key to their formation and explains observed lag times and size distributions.

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

Observation of a Pronounced Hebel-Slichter Peak in the Spin-Lattice Relaxation Rate and Implications for Gap and Pairing Symmetry in LaNiGa_{2}.

Physical review letters·2026
Same author

Spin Echo, Fidelity, and the Quantum Critical Fan in TmVO_{4}.

Physical review letters·2024
Same author

de Almeida-Thouless instability in short-range Ising spin glasses.

Physical review. E·2018
Same author

Tricriticality in crossed Ising chains.

Physical review. E·2018
Same author

Publisher's Note: Critical and Griffiths-McCoy singularities in quantum Ising spin glasses on d-dimensional hypercubic lattices: A series expansion study [Phys. Rev. E 96, 022139 (2017)].

Physical review. E·2018
Same author

Critical and Griffiths-McCoy singularities in quantum Ising spin glasses on d-dimensional hypercubic lattices: A series expansion study.

Physical review. E·2017

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Mammalian prion proteins (PrP) are a public health concern.
  • Yeast proteins, such as SUP35, mimic PrP misfolding and aggregation but are non-pathogenic.
  • Yeast prions offer a simpler system for studying protein misfolding dynamics.

Purpose of the Study:

  • To model the in vitro aggregation kinetics of the yeast SUP35 protein.
  • To explain observed phenomena: long aggregates, exponential growth, and weak dependence of lag time on monomer concentration.
  • To elucidate the role of aggregate fissioning in prion formation.

Main Methods:

  • Extended a previous aggregation kinetics model with a stochastic approach.
  • Incorporated aggregate fissioning and an initial nucleation barrier.

Related Experiment Videos

  • Analyzed in vitro experimental data for SUP35 protein aggregation.

    • Main Results:

    • The extended model successfully reproduced exponential growth, long aggregates, and weak lag time dependence on monomer concentration.
    • Low nucleation rates or seeding with preformed nuclei were critical for achieving these results.
    • Aggregate size distribution was accurately described by the Weibull distribution.

    Conclusions:

    • Aggregate fissioning plays a crucial role in the growth of misfolded proteins, particularly yeast prions.
    • The model provides a framework for understanding prion-like protein aggregation.
    • Findings contribute to the study of protein misfolding diseases.