Wang Q W, Kline A D, Wüthrich K
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Zürich-Hönggerberg, Switzerland.
Biochemistry. 1987 Oct 6;26(20):6488-93. doi: 10.1021/bi00394a030.
The individual amide proton exchange rates in Tendamistat at pH 3.0 and 50 degrees C were measured by using two-dimensional 1H nuclear magnetic resonance. Overall, it was found that the distribution of exchange rates along the sequence is dominated by the interstrand hydrogen bonds of the beta-sheet structures. The slowly exchanging protons in the core of the two beta-sheets were shown to exchange via an EX2 mechanism. Further analysis of the data indicates that different large-scale structure fluctuations are responsible for the exchange from the two beta-sheets, even though the three-dimensional structure of Tendamistat appears to consist of a single structural domain.
在pH 3.0和50℃条件下，通过二维¹H核磁共振测量了腱糖淀粉酶中各个酰胺质子的交换速率。总体而言，发现沿序列的交换速率分布主要由β-折叠结构的链间氢键主导。两个β-折叠核心中交换缓慢的质子通过EX2机制进行交换。对数据的进一步分析表明，尽管腱糖淀粉酶的三维结构似乎由单个结构域组成，但来自两个β-折叠的交换是由不同的大规模结构波动引起的。
