Journal of the American Chemical Society
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.
Copyright © 2007 American Chemical Society
American Chemical Society
Amides, Protein structure, Differential scanning calorimetry, Nuclear magnetic resonance spectroscopy, Stability
National Institutes of Health and the National Foundation for Cancer Research
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.