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An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies

An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1859483191

An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies

About this item

Full title

An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies

Publisher

London: Nature Publishing Group UK

Journal title

Nature chemistry, 2017-01, Vol.9 (1), p.39-44

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Amyloidogenic peptides and proteins play a crucial role in a variety of neurodegenerative disorders such as Alzheimer's and Parkinson's disease. These proteins undergo a spontaneous transition from a soluble, often partially folded form, into insoluble amyloid fibrils that are rich in β-sheets. Increasing evidence suggests that highly dynamic, poly...

Alternative Titles

Full title

An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_1859483191

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1859483191

Other Identifiers

ISSN

1755-4330

E-ISSN

1755-4349

DOI

10.1038/nchem.2615

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