Pressure stability of the α‐helix structure in a de novo designed protein (α‐l‐α)2 studied by FTIR spectroscopy
Pressure stability of the α‐helix structure in a de novo designed protein (α‐l‐α)2 studied by FTIR spectroscopy
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DOI：
10.1002/bip.20628
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发表时间：
2007-02
期刊：
影响因子：
2.9
通讯作者：
T. Takekiyo;N. Takeda;Y. Isogai;Minoru Katō;Y. Taniguchi
中科院分区：
文献类型：
--
作者：
T. Takekiyo;N. Takeda;Y. Isogai;Minoru Katō;Y. Taniguchi
用傅立叶变换红外光谱（FTIR）研究了一种全新设计的四螺旋束蛋白（α -l- α）(2)在水溶液中的压力诱导结构变化。酰胺I带强度的变化表明，压力诱导了三级相互作用的破坏，并稳定了溶剂化的α -螺旋形式。这可能表明疏水核心通过压力暴露于溶剂并不是压力诱导蛋白质展开α螺旋的充分条件。
The pressure-induced structural changes of a de novo designed four-helix bundle protein, (alpha-l-alpha)(2), in aqueous solution have been investigated by FTIR spectroscopy. Changes in the amide I' band intensity show that pressure induces disruption of tertiary interactions and stabilizes the solvated alpha-helical form. This may suggest that the exposure of the hydrophobic core to the solvent by pressure is not a sufficient condition for pressure-induced unfolding of the alpha-helices of proteins.