Document Type
Article
Publication Date
1-19-2007
Publication Source
Journal of the American Chemical Society
Abstract
We recently reported that β-peptides can form discrete hetero-oligomers in aqueous solution. Here we describe the structure of such an oligomer as determined by X-ray crystallography. The structure of Zwit-1F reveals a homo-octamer of two cupped “hands” composed of both parallel and antiparallel 314-helices. The core of the assembly is composed entirely of solvent-excluded β3-homoleucine residues. The Zwit-1F assembly shares many of the physical characteristics of natural proteins.
Inclusive pages
1532-1533
ISBN/ISSN
0002-7863
Document Version
Postprint
Copyright
Copyright © 2007 American Chemical Society
Publisher
American Chemical Society
Volume
129
Peer Reviewed
yes
Issue
6
Sponsoring Agency
National Institutes of Health and the National Foundation for Cancer Research
eCommons Citation
Daniels, Douglas S.; Petersson, E. James; Qiu, Jade X.; and Schepartz, Alanna S., "High-Resolution Structure of a Beta-Peptide Bundle" (2007). Chemistry Faculty Publications. 89.
https://ecommons.udayton.edu/chm_fac_pub/89
Comments
The document available for download is the authors' accepted manuscript, provided in compliance with the publisher's policy on self-archiving. Permission documentation is on file. To view the version of record, use the DOI provided.
Featured in: Borman, S. "Synthetic protein mimics the real thing." Chemical and Engineering News Vol. 85 (2007), 7.
Featured in: Borman, S. "2007 Chemistry Highlights." Chemical and Engineering News Vol. 85 (2007), 13-19.