Internal and environmental effects on folding and dimerisation of Alzheimer's β-amyloid peptide
Document Type
Article
Publication Date
5-1-2011
Abstract
Amyloid deposits are a hallmark of many diseases. In the case of Alzheimer's disease, a turn between 21Ala and 30Ala, stabilised by a salt bridge between 22Glu/23Asp and 28Lys, may nucleate folding and aggregation of the amyloid β(Aβ) peptide. In the present paper, we test this hypothesis by studying how salt bridge and turn formation vary with intrinsic and environmental changes, and how these changes affect folding and aggregation of the Aβ-peptide. © 2011 Taylor & Francis.
Publication Title
Molecular Simulation
Recommended Citation
Anand, P.,
&
Hansmann, U.
(2011).
Internal and environmental effects on folding and dimerisation of Alzheimer's β-amyloid peptide.
Molecular Simulation,
37(6), 440-448.
http://doi.org/10.1080/08927022.2011.551879
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p/9315