Spontaneous beta-barrel formation: an all-atom study of Abeta(16-22) oligomerization
Irbäck, Anders LU
and Mitternacht, Simon
LU
(2008)
In Proteins
71(1).
p.207-214
- Abstract
- Using all-atom Monte Carlo simulations with implicit water, combined with a cluster size analysis, we study the aggregation of A16-22, a peptide capable of forming amyloid fibrils. We consider a system of six initially randomly oriented A16-22 peptides, and investigate the thermodynamics and structural properties of aggregates formed by this system. The system is unaggregated without ordered secondary structure at high temperature, and forms -sheet rich aggregates at low temperature. At the crossover between these two regimes, we find that clusters of all sizes occur, whereas the -strand content is low. In one of several runs, we observe the spontaneous formation of a -barrel with six antiparallel strands. The -barrel stands out as the by... (More)
- Using all-atom Monte Carlo simulations with implicit water, combined with a cluster size analysis, we study the aggregation of A16-22, a peptide capable of forming amyloid fibrils. We consider a system of six initially randomly oriented A16-22 peptides, and investigate the thermodynamics and structural properties of aggregates formed by this system. The system is unaggregated without ordered secondary structure at high temperature, and forms -sheet rich aggregates at low temperature. At the crossover between these two regimes, we find that clusters of all sizes occur, whereas the -strand content is low. In one of several runs, we observe the spontaneous formation of a -barrel with six antiparallel strands. The -barrel stands out as the by far most long-lived aggregate seen in our simulations. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/796135
- author
- Irbäck, Anders
LU
and Mitternacht, Simon
LU
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- protein aggregation, self-assembly, cluster size analysis, amyloid-, protein misfolding
- in
- Proteins
- volume
- 71
- issue
- 1
- pages
- 207 - 214
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000254035500020
- scopus:40549089901
- pmid:17932914
- ISSN
- 0887-3585
- DOI
- 10.1002/prot.21682
- language
- English
- LU publication?
- yes
- id
- e26d54c9-4c11-4ae7-8b75-05be99ce9409 (old id 796135)
- date added to LUP
- 2016-04-01 13:13:24
- date last changed
- 2024-04-10 02:15:17
@article{e26d54c9-4c11-4ae7-8b75-05be99ce9409,
abstract = {{Using all-atom Monte Carlo simulations with implicit water, combined with a cluster size analysis, we study the aggregation of A16-22, a peptide capable of forming amyloid fibrils. We consider a system of six initially randomly oriented A16-22 peptides, and investigate the thermodynamics and structural properties of aggregates formed by this system. The system is unaggregated without ordered secondary structure at high temperature, and forms -sheet rich aggregates at low temperature. At the crossover between these two regimes, we find that clusters of all sizes occur, whereas the -strand content is low. In one of several runs, we observe the spontaneous formation of a -barrel with six antiparallel strands. The -barrel stands out as the by far most long-lived aggregate seen in our simulations.}},
author = {{Irbäck, Anders and Mitternacht, Simon}},
issn = {{0887-3585}},
keywords = {{protein aggregation; self-assembly; cluster size analysis; amyloid-; protein misfolding}},
language = {{eng}},
number = {{1}},
pages = {{207--214}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Proteins}},
title = {{Spontaneous beta-barrel formation: an all-atom study of Abeta(16-22) oligomerization}},
url = {{http://dx.doi.org/10.1002/prot.21682}},
doi = {{10.1002/prot.21682}},
volume = {{71}},
year = {{2008}},
}