Leo G C, Colnago L A, Valentine K G, Opella S J
Biochemistry. 1987 Feb 10;26(3):854-62. doi: 10.1021/bi00377a029.
The dynamics of backbone and side-chain sites of the membrane-bound form of fd coat protein are described with solid-state 2H and 15N NMR experiments. The samples were isotopically labeled coat protein in phospholipid bilayers in excess water. The protein itself is immobile and does not undergo rapid rotation within the bilayer. Like the structural form of the protein, the membrane-bound form has four mobile residues at the N-terminus. The membrane-bound form differs from the structural form in having several mobile residues at the C-terminus. Many of the side chains of residues with immobile backbone sites undergo large amplitude jump motions. The dynamics are generally similar in both the structural and membrane-bound forms of the protein.
通过固态2H和15N核磁共振实验描述了fd外壳蛋白膜结合形式的主链和侧链位点的动力学。样品是在过量水中磷脂双层中的同位素标记外壳蛋白。蛋白质本身是固定的，不会在双层内快速旋转。与蛋白质的结构形式一样，膜结合形式在N端有四个可移动残基。膜结合形式与结构形式的不同之处在于C端有几个可移动残基。许多主链位点固定的残基的侧链会进行大幅度跳跃运动。蛋白质的结构形式和膜结合形式的动力学通常相似。
