Hydrogen−Deuterium Exchange of Streptavidin and Its Complex with Biotin Studied by 2D-Attenuated Total Reflection Fourier Transform Infrared Spectroscopy
Hydrogen−Deuterium Exchange of Streptavidin and Its Complex with Biotin Studied by 2D-Attenuated Total Reflection Fourier Transform Infrared Spectroscopy
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DOI：
10.1021/ja984208k
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发表时间：
1999-05
影响因子：
15
通讯作者：
S. Meskers;J. Ruysschaert;E. Goormaghtigh
中科院分区：
文献类型：
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作者：
S. Meskers;J. Ruysschaert;E. Goormaghtigh
利用衰减全反射傅里叶变换红外光谱研究了链霉亲和素及其生物素复合物的氢氘交换反应。为了分析氘化后的光谱变化，计算了差谱和二维相关谱。我们发现，交换率随二级结构而变化，其中交换酰胺质子被纳入。交换最慢的质子，其特征时间常数约为小时，是β折叠二级结构的一部分。β-折叠与其他结构元件交换时的分离允许鉴定β-折叠的酰胺II和II'频率（1530和1445 cm-1）。第二种组分的交换速度比β折叠快，其酰胺I频率为1680、1640和1465 cm-1。该组分归因于除中心β-桶之外的二级结构中的酰胺基团的交换。配体受体的结合。
Hydrogen−deuterium exchange for streptavidin and its complex with biotin is studied by means of attenuated total reflection (ATR) Fourier transform infrared (FTIR) spectroscopy. To analyze the spectral changes upon deuteration, difference spectra and two-dimensional correlation spectra are calculated. We find that the exchange rate varies with the secondary structure in which the exchanging amide protons are incorporated. The most slowly exchanging protons, with a characteristic time constant on the order of hours, are part of the β-sheet secondary structure. The separation in time of exchange of the β-sheet from other structural elements allows the amide II and II‘ frequencies of the β-sheet (1530 and 1445 cm-1) to be identified. A second component which exchanges more rapidly than the β-sheet is characterized by its amide I frequencies 1680, 1640, and 1465 cm-1. This component is attributed to the exchange of amide groups in secondary structures other than the central β-barrel. Binding of the ligand res...