In:
Communications in Theoretical Physics, IOP Publishing, Vol. 71, No. 9 ( 2019-09-01), p. 1121-
Abstract:
One major cause of Alzheimer’s disease (AD) is evidently due to the aggregation and deposition of amyloid β peptides (A β ) in the brain tissue of the patient. Preventing misfolding and self-aggregation of A β protein can reduce the formation of highly toxic polymer, which is important for the treatment of AD. Among them, the α -helix consisting of 42 residues (A β 42) is the main component of senile plaques in AD. In this paper, 500 ns accelerated molecular dynamics are performed at different temperatures (300 K, 350 K, 400 K, 450 K) to study of the effect of temperature-induced conformation changes of A β 42 protein during the unfolding process respectively.
Type of Medium:
Online Resource
ISSN:
0253-6102
,
1572-9494
DOI:
10.1088/0253-6102/71/9/1121
Language:
Unknown
Publisher:
IOP Publishing
Publication Date:
2019
detail.hit.zdb_id:
2021522-8
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