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The Protofilament Structure of Insulin Amyloid Fibrils

The Protofilament Structure of Insulin Amyloid Fibrils

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_citationtrail_10_1073_pnas_142459399

The Protofilament Structure of Insulin Amyloid Fibrils

About this item

Full title

The Protofilament Structure of Insulin Amyloid Fibrils

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2002-07, Vol.99 (14), p.9196-9201

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Under solution conditions where the native state is destabilized, the largely helical polypeptide hormone insulin readily aggregates to form amyloid fibrils with a characteristic cross-β structure. However, there is a lack of information relating the 4.8 Å, β-strand repeat to the higher order assembly of amyloid fibrils. We have used cryo-electron...

Alternative Titles

Full title

The Protofilament Structure of Insulin Amyloid Fibrils

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_crossref_citationtrail_10_1073_pnas_142459399

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_citationtrail_10_1073_pnas_142459399

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.142459399

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