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Self-Assembly of Microtubule Tactoids
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Stochastic lag time in nucleated linear self-assembly.

Nitin S Tiwari1, Paul van der Schoot1

  • 1Group Theory of Polymers and Soft Matter, Eindhoven University of Technology, P.O. Box 513, 5600 MB Eindhoven, The Netherlands.

The Journal of Chemical Physics
|June 24, 2016
PubMed
Summary
This summary is machine-generated.

Protein aggregation, like amyloid fibrillation, involves stochastic processes at the cellular level. This study shows that the lag time before self-assembly begins is inversely proportional to system volume for larger systems.

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Area of Science:

  • Biochemistry
  • Chemical Physics
  • Computational Biology

Background:

  • Protein aggregation is crucial in biological processes, including amyloid fibrillation.
  • Cellular-scale aggregation is inherently stochastic due to statistical number fluctuations in small systems.

Purpose of the Study:

  • To investigate the nucleated reversible self-assembly of monomers into polymer-like aggregates.
  • To analyze the impact of stochastic fluctuations on polymerization reactions.
  • To focus on the lag phase preceding self-assembly and its associated lag time.

Main Methods:

  • Utilizing the kinetic Monte Carlo method, which inherently models stochastic processes.
  • Studying the lag time as a function of system size and kinetic pathway.

Main Results:

  • The leading order stochastic contribution to the lag time is inversely proportional to system volume for sufficiently large systems.
  • This inverse relationship holds across all nine reaction pathways examined.
  • Finite-size corrections to the lag time exhibit dependence on the specific kinetic pathway.

Conclusions:

  • Stochastic effects significantly influence the lag phase in protein self-assembly.
  • System size is a critical factor determining the lag time, with an inverse relationship observed for larger volumes.
  • Understanding these stochastic contributions is essential for comprehending protein aggregation dynamics.