Contribution to a conference proceedings/Journal Article

FZJ-2013-05166

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Monte Carlo Studies of Protein Aggregation

Jónsson, S. Æ. ; Staneva, I. ; Mohanty, S.FZJ* ; Irbäck, A. (Corresponding author)

2012
Elsevier Amsterdam [u.a.]

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Please use a persistent id in citations: doi:10.1016/j.phpro.2012.05.008

Abstract: The disease-linked amyloid β (Aβ) and α-synuclein (αS) proteins are both fibril-forming and natively unfolded in free monomeric form. Here, we discuss two recent studies, where we used extensive implicit solvent all-atom Monte Carlo (MC) simulations to elucidate the conformational ensembles sampled by these proteins. For αS, we somewhat unexpectedly observed two distinct phases, separated by a clear free-energy barrier. The presence of the barrier makes αS, with 140 residues, a challenge to simulate. By using a two-step simulation procedure based on flat-histogram techniques, it was possible to alleviate this problem. The barrier may in part explain why fibril formation is much slower for αS than it is for Aβ.

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Contributing Institute(s):

1. Jülich Supercomputing Center (JSC)

Research Program(s):

1. 411 - Computational Science and Mathematical Methods (POF2-411) (POF2-411)

Appears in the scientific report 2013

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