期刊
APPLIED PHYSICS LETTERS
卷 94, 期 24, 页码 -出版社
AMER INST PHYSICS
DOI: 10.1063/1.3148641
关键词
diseases; hydrogen bonds; molecular biophysics; molecular configurations; proteins
资金
- Office of Naval Research [NN-00014-08-01-0844]
Amyloid fibril formation and characterization are crucial due to their association with severe degenerative disorders such as Alzheimer's, type II diabetes, and Parkinson's disease. Here we present an atomistic-based multiscale analysis, utilized to predict the structure of Alzheimer A beta(1-40) fibrils. Our study provides a structural model of amyloid fibers with lengths of hundreds of nanometers at atomistic resolution. We report a systematic analysis of the energies, structural changes and H-bonding for varying fibril lengths, elucidating their size dependent properties. Our model predicts the formation of twisted amyloid microfibers with a periodicity of approximate to 82 nm, in close agreement with experimental results.
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