Laboratoire de Radiolyse, SIS2M, IRAMIS, UMR3299 CEA-CNRS , 91191 Gif-sur-Yvette, France.
Langmuir. 2013 Nov 5;29(44):13465-72. doi: 10.1021/la4035479. Epub 2013 Oct 21.
If protein structure and function changes upon adsorption are well documented, modification of adsorbed protein dynamics remains a blind spot, despite its importance in biological processes. The adsorption of metmyoglobin on a silica surface was studied by isotherm measurements, microcalorimetry, circular dichroïsm, and UV-visible spectroscopy to determine the thermodynamic parameters of protein adsorption and consequent structure modifications. The mean square displacement and the vibrational densities of states of the adsorbed protein were measured by elastic and inelastic neutron scattering experiments. A decrease of protein flexibility and depletion in low frequency modes of myoglobin after adsorption on silica was observed. Our results suggest that the structure loss itself is not the entropic driving force of adsorption.
如果蛋白质结构和功能在吸附后发生变化有充分的记录，那么尽管在生物过程中非常重要，吸附蛋白质动力学的修饰仍然是一个盲点。通过等温测量、微量热法、圆二色性和紫外可见光谱研究了肌红蛋白在二氧化硅表面的吸附，以确定蛋白质吸附的热力学参数和随之而来的结构修饰。通过弹性和非弹性中子散射实验测量了吸附蛋白质的均方位移和振动态密度。观察到肌红蛋白在二氧化硅上吸附后蛋白质柔韧性降低和低频模式耗散。我们的结果表明，结构损失本身不是吸附的熵驱动力。
