Stabilities and Conformations of Alzheimer's β-Amyloid Peptide Oligomers (Aβ16-22, Aβ16-35, and Aβ10...
Stabilities and Conformations of Alzheimer's β-Amyloid Peptide Oligomers (Aβ16-22, Aβ16-35, and Aβ10-35): Sequence Effects
About this item
Full title
Author / Creator
Publisher
United States: National Academy of Sciences
Journal title
Language
English
Formats
Publication information
Publisher
United States: National Academy of Sciences
Subjects
More information
Scope and Contents
Contents
Previously, we have studied the minimal oligomer size of an aggregate amyloid seed and the mechanism of seed growth with a multilayer β-sheet model. Under high temperature simulation conditions, our approach can test the stability of possible amyloid forms. Here, we report our study of oligomers of Alzheimer's amyloid β-peptide (Aβ) fragments 16-22...
Alternative Titles
Full title
Stabilities and Conformations of Alzheimer's β-Amyloid Peptide Oligomers (Aβ16-22, Aβ16-35, and Aβ10-35): Sequence Effects
Authors, Artists and Contributors
Author / Creator
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_proquest_miscellaneous_72638374
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_72638374
Other Identifiers
ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.212206899