Saudek V, Williams R J, Ramponi G
Inorganic Chemistry Laboratory, University of Oxford, England.
FEBS Lett. 1989 Jan 2;242(2):225-32. doi: 10.1016/0014-5793(89)80474-0.
The solution structure of acylphosphatase determined by proton nuclear magnetic resonance spectroscopy is described. The results allow us to discuss the fold of the protein (101 amino acids), to correlate the exposure and the mobility of the backbone with the antigenicity, and to locate the active site.
本文描述了通过质子核磁共振光谱法测定的酰基磷酸酶的溶液结构。这些结果使我们能够讨论该蛋白质(101个氨基酸)的折叠情况,将主链的暴露程度和流动性与抗原性相关联,并确定活性位点的位置。