蛋白质络合对Im9机械稳定性的影响。
The effect of protein complexation on the mechanical stability of Im9.
作者信息
Hann Eleanore, Kirkpatrick Nadine, Kleanthous Colin, Smith D Alastair, Radford Sheena E, Brockwell David J
机构信息
Institute of Molecular and Cellular Biology, University of Leeds, United Kingdom.
出版信息
Biophys J. 2007 May 1;92(9):L79-81. doi: 10.1529/biophysj.106.102475. Epub 2007 Mar 9.
Abstract
Force mode microscopy can be used to examine the effect of mechanical manipulation on the noncovalent interactions that stabilize proteins and their complexes. Here we describe the effect of complexation by the high affinity protein ligand E9 on the mechanical resistance of the simple four-helical protein, Im9. When concatenated into a construct of alternating I27 domains, Im9 unfolded below the thermal noise limit of the instrument ( approximately 20 pN). Complexation of E9 had little effect on the mechanical resistance of Im9 (unfolding force approximately 30 pN) despite the high avidity of this complex (K(d) approximately 10 fM).
摘要
力模式显微镜可用于研究机械操作对稳定蛋白质及其复合物的非共价相互作用的影响。在此，我们描述了高亲和力蛋白质配体E9的复合作用对简单四螺旋蛋白质Im9机械抗性的影响。当连接成交替的I27结构域构建体时，Im9在仪器的热噪声极限（约20 pN）以下展开。尽管该复合物具有高亲和力（K(d)约为10 fM），但E9的复合对Im9的机械抗性影响很小（展开力约为30 pN）。
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