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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...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_72638374

Stabilities and Conformations of Alzheimer's β-Amyloid Peptide Oligomers (Aβ16-22, Aβ16-35, and Aβ10-35): Sequence Effects

About this item

Full title

Stabilities and Conformations of Alzheimer's β-Amyloid Peptide Oligomers (Aβ16-22, Aβ16-35, and Aβ10-35): Sequence Effects

Author / Creator

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2002-10, Vol.99 (22), p.14126-14131

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

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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

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

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