Biophysical characterization of a β-peptide bundle:: Comparison to natural proteins
Biophysical characterization of a β-peptide bundle:: Comparison to natural proteins
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DOI：
10.1021/ja070567g
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发表时间：
2007-05-02
影响因子：
15
通讯作者：
Schepartz, Alanna
中科院分区：
文献类型：
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作者：
Petersson, E. James;Craig, Cody J.;Schepartz, Alanna
我们最近描述了由8个β肽Zwit-1F拷贝组成的螺旋束的高分辨率X射线结构。与自然界中的许多蛋白质一样，Zwit-1F八聚体包含平行和反平行螺旋、广泛的螺旋间静电相互作用和不含溶剂的疏水性核心。在这里，我们探索的Zwit-1F八聚体的稳定性，使用圆二色谱（CD）光谱，分析超离心（Au），差示扫描量热法（DSC），和NMR。这些研究表明，Zwit-1F的热力学和动力学性质与α-螺旋束蛋白非常相似。总之，这些研究应该提供一个模型的设计β-肽蛋白的生物功能。
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.