Trewhella J
Life Sciences Division, Los Alamos National Laboratory, New Mexico.
Cell Calcium. 1992 Jun-Jul;13(6-7):377-90. doi: 10.1016/0143-4160(92)90051-s.
Small-angle X-ray and neutron scattering experiments have given important information on the solution structures of calmodulin and its complexes with synthetic peptides used to model target enzyme interactions. In combination with crystallographic data, site directed mutagenesis and various spectroscopic studies, these experiments have contributed to our understanding of the solution structure of calmodulin in different functional states. We have gained important insights into the conformational flexibility in calmodulin that appears to be crucial to its regulatory functions. Specifically, flexibility in the interconnecting helix region of calmodulin has been shown to play a critical role in facilitating calmodulin's binding to a wide variety of target enzymes whose activities are thus regulated. This review will focus mainly on the contributions small-angle scattering has made to our understanding of the solution structure of calmodulin in the context of other studies, with particular regard to circular dichroism and Fourier transform infrared studies that complement the small-angle scattering data.
小角X射线和中子散射实验提供了有关钙调蛋白及其与用于模拟靶酶相互作用的合成肽复合物的溶液结构的重要信息。结合晶体学数据、定点诱变和各种光谱研究，这些实验有助于我们理解处于不同功能状态的钙调蛋白的溶液结构。我们对钙调蛋白的构象灵活性有了重要的认识，这似乎对其调节功能至关重要。具体而言，已证明钙调蛋白相互连接螺旋区域的灵活性在促进钙调蛋白与多种靶酶结合方面起着关键作用，这些靶酶的活性因此受到调节。本综述将主要关注小角散射在其他研究背景下对我们理解钙调蛋白溶液结构所做的贡献，特别是关于补充小角散射数据的圆二色性和傅里叶变换红外研究。
