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A minimalistic model for peptide fibril formation

Linnemann, Niels Siegbert LU (2012) FYTK01 20121
Computational Biology and Biological Physics
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.
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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},
  keyword      = {fibril,fibril formation,protein physics,amyloid fibril,model for fibril formation},
  language     = {eng},
  note         = {Student Paper},
  title        = {A minimalistic model for peptide fibril formation},
  year         = {2012},
}