McDowell L M, Schaefer J
Department of Chemistry, Washington University, St Louis, MO 63130, USA.
Curr Opin Struct Biol. 1996 Oct;6(5):624-9. doi: 10.1016/s0959-440x(96)80028-5.
Solid-state NMR experiments have recently provided a number of biochemical insights: motionally averaged 2H lineshapes have shown that the motion of a backbone loop protecting a protein binding site is not ligand gated; isotropic 13C chemical shifts of freeze-quenched enzyme-ligand intermediates have revealed mechanistic details of reaction pathways; multiple heteronuclear distance determinations have characterized the binding-site geometry of a 46 kDa noncrystalline enzyme complex; and homonuclear recoupling experiments have established that insoluble amyloid fibrils form a pleated beta sheet.
动态平均的2H线形表明，保护蛋白质结合位点的主链环的运动不是由配体门控的；冷冻淬灭的酶-配体中间体的各向同性13C化学位移揭示了反应途径的机制细节；多次异核距离测定确定了一种46 kDa非晶态酶复合物的结合位点几何结构；同核重耦合实验证实不溶性淀粉样原纤维形成了褶皱的β-折叠片层。
