NMR studies of amyloid β-peptides: proton assignments, secondary structure, and mechanism of an α-helix-β-sheet conversion for a homologous, 28-residue, N-terminal fragment

Zagorski, Michael G and Barrow, Colin J 1992, NMR studies of amyloid β-peptides: proton assignments, secondary structure, and mechanism of an α-helix-β-sheet conversion for a homologous, 28-residue, N-terminal fragment, Biochemistry, vol. 31, no. 24, pp. 5621-5631, doi: 10.1021/bi00139a028.

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Title NMR studies of amyloid β-peptides: proton assignments, secondary structure, and mechanism of an α-helix-β-sheet conversion for a homologous, 28-residue, N-terminal fragment
Author(s) Zagorski, Michael G
Barrow, Colin JORCID iD for Barrow, Colin J orcid.org/0000-0002-2153-7267
Journal name Biochemistry
Volume number 31
Issue number 24
Start page 5621
End page 5631
Total pages 11
Publisher American Chemical Society
Place of publication Washington, D.C.
Publication date 1992
ISSN 0006-2960
1520-4995
Language eng
DOI 10.1021/bi00139a028
Indigenous content off
Field of Research 0601 Biochemistry and Cell Biology
1101 Medical Biochemistry and Metabolomics
0304 Medicinal and Biomolecular Chemistry
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©1992, American Chemical Society
Persistent URL http://hdl.handle.net/10536/DRO/DU:30126527

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