期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 129, 期 17, 页码 5344-+出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja070567g
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资金
- NIGMS NIH HHS [R01 GM074756-04, R01 GM074756] Funding Source: Medline
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.
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