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A minimalistic model for peptide fibril formation

Linnemann, Niels Siegbert LU (2012) FYTK01 20121
Computational Biology and Biological Physics - Undergoing reorganization
Abstract
A lattice model for fibril formation on the basis of general peptide interactions is presented. Fibrils are well-structured protein aggregates and a key phenomenon in many diseases, among them Alzheimer.
We study the model’s equilibrium and kinetic properties using Wang-Landau sampling and a Metropolis Monte Carlo algorithm with cluster moves. The peptides are shown to form ordered fibrilar aggregates at low temperatures, while being non-aggregated at high temperatures. A sharp
transition separates the two phases. In the kinetic simulations, the growth of fibrils is associated with two lag phases.
Please use this url to cite or link to this publication:
author
Linnemann, Niels Siegbert LU
supervisor
organization
course
FYTK01 20121
year
type
M2 - Bachelor Degree
subject
keywords
fibril, fibril formation, protein physics, amyloid fibril, model for fibril formation
language
English
id
2796876
date added to LUP
2013-01-25 09:08:14
date last changed
2017-10-06 16:44:14
@misc{2796876,
  abstract     = {{A lattice model for fibril formation on the basis of general peptide interactions is presented. Fibrils are well-structured protein aggregates and a key phenomenon in many diseases, among them Alzheimer.
We study the model’s equilibrium and kinetic properties using Wang-Landau sampling and a Metropolis Monte Carlo algorithm with cluster moves. The peptides are shown to form ordered fibrilar aggregates at low temperatures, while being non-aggregated at high temperatures. A sharp
transition separates the two phases. In the kinetic simulations, the growth of fibrils is associated with two lag phases.}},
  author       = {{Linnemann, Niels Siegbert}},
  language     = {{eng}},
  note         = {{Student Paper}},
  title        = {{A minimalistic model for peptide fibril formation}},
  year         = {{2012}},
}