Barth A, Zscherp C
Institut für Biophysik, Johann Wolfgang Goethe-Universität, Theodor-Stern-Kai 7, Haus 74, D-60590, Frankfurt am Main, Germany.
FEBS Lett. 2000 Jul 21;477(3):151-6. doi: 10.1016/s0014-5793(00)01782-8.
Protein conformational changes triggered by molecule binding are increasingly investigated by infrared spectroscopy often using caged compounds. Several examples of molecule-protein recognition studies are given, which focus on nucleotide binding to proteins. The investigation of enzyme mechanisms is illustrated in detail using the Ca(2+)-ATPase of the sarcoplasmic reticulum membrane as an example. It is shown that infrared spectroscopy provides valuable information on general aspects of enzyme function as well as on molecular details of molecule-protein interactions and the mechanism of catalysis.
由分子结合引发的蛋白质构象变化越来越多地通过红外光谱法进行研究,通常会使用笼形化合物。文中给出了几个分子 - 蛋白质识别研究的例子,这些研究聚焦于核苷酸与蛋白质的结合。以肌质网膜的Ca(2 +)-ATP酶为例,详细说明了对酶机制的研究。结果表明,红外光谱法在酶功能的一般方面以及分子 - 蛋白质相互作用的分子细节和催化机制方面都提供了有价值的信息。