通过圆二色光谱法对金黄色葡萄球菌蛋白A二级结构的估计。
Estimation of the secondary structure of protein A from S. aureus by CD-spectroscopy.
作者信息
Lindmark R
出版信息
Mol Immunol. 1982 Jul;19(7):957-9. doi: 10.1016/0161-5890(82)90361-3.
PMID:7121471
Abstract
The secondary structure of protein A(SpA) was estimated to 31% alpha-helix, 13% beta-structure and 56% random coil by CD-spectroscopy, which is close to the sum of the secondary structures of the SpA fragments. This supports that the SpA molecule is composed N-terminally of four Fc-binding units each consisting of two antiparallel alpha-helices interconnected by random coil segments and C-terminally of an region mainly in random coil.
摘要
通过圆二色光谱法估计，蛋白A（SpA）的二级结构为31%的α-螺旋、13%的β-结构和56%的无规卷曲，这与SpA片段二级结构的总和相近。这支持了SpA分子在N端由四个Fc结合单元组成，每个单元由两个通过无规卷曲片段相互连接的反平行α-螺旋组成，在C端主要是一个无规卷曲区域。
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