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Quenched hydrogen-deuterium exchange NMR of a disease-relevant A[beta]

Quenched hydrogen-deuterium exchange NMR of a disease-relevant A[beta]

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_gale_incontextgauss_ISR_A486217860

Quenched hydrogen-deuterium exchange NMR of a disease-relevant A[beta]

About this item

Full title

Quenched hydrogen-deuterium exchange NMR of a disease-relevant A[beta]

Publisher

Public Library of Science

Journal title

PloS one, 2017-03, Vol.12 (3), p.e0172862

Language

English

Formats

Publication information

Publisher

Public Library of Science

More information

Scope and Contents

Contents

Alzheimer's disease is associated with the aggregation into amyloid fibrils of A[beta](1-42) and A[beta](1-40) peptides. Interestingly, these fibrils often do not obtain one single structure but rather show different morphologies, so-called polymorphs. Here, we compare quenched hydrogen-deuterium (H/D) exchange of a disease-relevant A[beta](1-42) f...

Alternative Titles

Full title

Quenched hydrogen-deuterium exchange NMR of a disease-relevant A[beta]

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_gale_incontextgauss_ISR_A486217860

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_gale_incontextgauss_ISR_A486217860

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0172862

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