Czuryło E A, Hellweg T, Eimer W, Dabrowska R
Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.
Biophys J. 1997 Feb;72(2 Pt 1):835-42. doi: 10.1016/s0006-3495(97)78717-4.
The size and the shape of caldesmon as well as its 50-kDa central and 19-kDa C-terminal fragments were investigated by photon correlation spectroscopy. The hydrodynamic radii, which have been calculated from the experimentally obtained translational diffusion coefficients, are 9.8 nm, 6.0 nm, and 2.9 nm, respectively. Moreover, the experimental values for the translational diffusion coefficients are compared with results obtained from hydrodynamic model calculations. Detailed models for the structure of caldesmon in solution are derived. The contour length is about 64 nm for all of the models used for caldesmon.
通过光子相关光谱法研究了钙调蛋白的大小、形状及其50 kDa的中央片段和19 kDa的C末端片段。根据实验获得的平移扩散系数计算出的流体动力学半径分别为9.8 nm、6.0 nm和2.9 nm。此外,将平移扩散系数的实验值与流体动力学模型计算结果进行了比较。推导了溶液中钙调蛋白结构的详细模型。所使用的所有钙调蛋白模型的轮廓长度约为64 nm。