Document Type
Article
Publication Date
4-11-2007
Publication Source
Journal of the American Chemical Society
Abstract
We recently described the high-resolution X-ray structure of a helical bundle composed of eight copies of the β-peptide Zwit-1F. Like many proteins in Nature, the Zwit-1F octamer contains parallel and antiparallel helices, extensive inter-helical electrostatic interactions, and a solvent-excluded hydrophobic core. Here we explore the stability of the Zwit-1F octamer using circular dichroism (CD) spectroscopy, analytical ultracentrifugation (AU), differential scanning calorimetry (DSC), and NMR. These studies demonstrate that the thermodynamic and kinetic properties of Zwit-1F closely resemble those of α-helical bundle proteins. Together these studies should provide a model for the design of β-peptide proteins with biological functions.
Inclusive pages
5344-5345
ISBN/ISSN
0002-7863
Document Version
Postprint
Copyright
Copyright © 2007 American Chemical Society
Publisher
American Chemical Society
Volume
129
Peer Reviewed
yes
Issue
17
Keywords
Amides, Protein structure, Differential scanning calorimetry, Nuclear magnetic resonance spectroscopy, Stability
Sponsoring Agency
National Institutes of Health and the National Foundation for Cancer Research
eCommons Citation
Petersson, E. James; Craig, Cody J.; Daniels, Douglas S.; Qiu, Jade X.; and Schepartz, Alanna S., "Biophysical Characterization of a Beta-Peptide Bundle: Comparison To Natural Proteins" (2007). Chemistry Faculty Publications. 90.
https://ecommons.udayton.edu/chm_fac_pub/90
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.