Bhattacharjee S, Glucksman M J, Makowski L
Department of Biochemistry and Molecular Biophysics, College of Physicians and Surgeons, Columbia University, New York, New York 10032.
Biophys J. 1992 Mar;61(3):725-35. doi: 10.1016/S0006-3495(92)81877-5.
Fiber diffraction studies are used to demonstrate that changes in the helical symmetry of the protein coat of filamentous bacterial viruses fd and M13 are correlated with changes in the surface charge. Comparison of the structure of M13 and fd at pH 2 and 8 indicate that surface charge affects both the helical symmetry and flexibility of the virions. The changes in helical symmetry are similar in magnitude to that observed in the Pseudomanas phage Pf1 and probably reflect an inocuous side effect of the particle flexibility required for protection of the virus particles from damage due to shear. The magnitude of the observed changes in helical symmetry appears to be limited to that which can occur without repacking of the interfaces between the alpha-helices making up the viral protein coat.
纤维衍射研究用于证明丝状细菌病毒fd和M13蛋白质衣壳的螺旋对称性变化与表面电荷变化相关。对M13和fd在pH 2和pH 8时结构的比较表明，表面电荷影响病毒粒子的螺旋对称性和柔韧性。螺旋对称性的变化幅度与在假单胞菌噬菌体Pf1中观察到的相似，可能反映了为保护病毒粒子免受剪切损伤所需的粒子柔韧性的无害副作用。观察到的螺旋对称性变化幅度似乎仅限于在不重新排列构成病毒蛋白质衣壳的α-螺旋之间的界面的情况下可能发生的变化。
