Lin Y, Nielsen R, Murray D, Hubbell W L, Mailer C, Robinson B H, Gelb M H
Department of Chemistry, Biochemistry, University of Washington, Box 351700, Seattle, WA 98195-1700, USA.
Science. 1998 Mar 20;279(5358):1925-9. doi: 10.1126/science.279.5358.1925.
A method involving electron paramagnetic resonance spectroscopy of a site-selectively spin-labeled peripheral membrane protein in the presence and absence of membranes and of a water-soluble spin relaxant (chromium oxalate) has been developed to determine how bee venom phospholipase A2 sits on the membrane. Theory based on the Poisson-Boltzmann equation shows that the rate of spin relaxation of a protein-bound nitroxide by a membrane-impermeant spin relaxant depends on the distance (up to tens of angstroms) from the spin probe to the membrane. The measurements define the interfacial binding surface of this secreted phospholipase A2.
已开发出一种方法，该方法涉及在有膜和无膜以及存在水溶性自旋弛豫剂（草酸铬）的情况下，对位点选择性自旋标记的外周膜蛋白进行电子顺磁共振光谱分析，以确定蜂毒磷脂酶A2如何位于膜上。基于泊松 - 玻尔兹曼方程的理论表明，膜不可渗透的自旋弛豫剂使与蛋白质结合的氮氧化物的自旋弛豫速率取决于从自旋探针到膜的距离（可达数十埃）。这些测量确定了这种分泌型磷脂酶A2的界面结合表面。
