Impact of Strand Number on Parallel β-Sheet Stability.
Impact of Strand Number on Parallel β-Sheet Stability.
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DOI：
10.1002/anie.201506448
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发表时间：
2015-11-23
期刊：
影响因子：
--
通讯作者：
Gellman SH
中科院分区：
文献类型：
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作者：
Kung VM;Cornilescu G;Gellman SH
我们通过比较水溶液中采用两股或三股平行β片构象的肽，研究了平行β片二级结构是否随着β链数量的增加而变得更加稳定。我们的三股设计是三股平行β片的第一个实验模型。通过核磁共振（NMR）和圆二色性（CD）光谱分析设计的肽支持这样的假设，即增加β-链的数量，从2到3，增加平行β-片的稳定性。我们提出了三链平行β片折叠中协同性的第一个实验证据，并展示了最小模型系统如何能够实现平行β片的特征特性（如CD光谱）的实验记录。
We have examined whether parallel β-sheet secondary structure becomes more stable as the number of β-strands increases, via comparisons among peptides designed to adopt two- or three-stranded parallel β-sheet conformations in aqueous solution. Our three-strand design is the first experimental model of a triple-stranded parallel β-sheet. Analysis of the designed peptides via nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy supports the hypothesis that increasing the number of β-strands, from two to three, increases the stability of the parallel β-sheet. We present the first experimental evidence for cooperativity in the folding of a triple-stranded parallel β-sheet, and we show how minimal model systems may enable experimental documentation of characteristic properties, such as CD spectra, of parallel β-sheets.