Liu Yun, Fratini Emiliano, Baglioni Piero, Chen Wei-Ren, Chen Sow-Hsin
Department of Nuclear Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Phys Rev Lett. 2005 Sep 9;95(11):118102. doi: 10.1103/PhysRevLett.95.118102. Epub 2005 Sep 8.
Small angle neutron scattering intensity distributions taken from cytochrome C and lysozyme protein solutions show a rising intensity at a very small wave vector Q, which can be interpreted in terms of the presence of a weak long-range attraction between protein molecules. This interaction has a range several times that of the diameter of the protein molecule, much greater than the range of the screened electrostatic repulsion. We show evidence that this long-range attraction is closely related to the type of anion present and ion concentration in the solution.
从小细胞色素C和溶菌酶蛋白质溶液中获取的小角中子散射强度分布显示,在非常小的波矢Q处强度上升,这可以解释为蛋白质分子之间存在弱的长程吸引力。这种相互作用的范围是蛋白质分子直径的几倍,远大于屏蔽静电排斥的范围。我们证明了这种长程吸引力与溶液中存在的阴离子类型和离子浓度密切相关。