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American Chemical Society, Journal of the American Chemical Society, 17(129), p. 5344-5345, 2007

DOI: 10.1021/ja070567g

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Biophysical Characterization of a β-Peptide Bundle: Comparison to Natural Proteins

Journal article published in 2007 by E. James Petersson, Cody J. Craig, Douglas S. Daniels ORCID, Jade X. Qiu, Alanna Schepartz
This paper is available in a repository.
This paper is available in a repository.

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Abstract

We recently described the high-resolution X-ray structure of a helical bundle composed of eight copies of the beta-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 alpha-helical bundle proteins. Together these studies should provide a model for the design of beta-peptide proteins with biological functions.