维吉尼亚霉素
化学
氯仿
50年代
晶体结构
结晶学
核糖体
立体化学
生物化学
色谱法
基因
核糖核酸
抗生素
作者
Jason Dang,Basti Bergdahl,Frances Separovic,Robert T. C. Brownlee,Robert P. Metzger
摘要
The conformation of virginiamycin M1 (VM1) in chloroform, determined by high-resolution NMR experiments, differs significantly from that of the X-ray crystal structure of VM1 bound to the 50S ribosome and to the active site of a streptogramin acetyltransferase enzyme. This implies that the binding process to these entities causes a major change in VM1 conformation.
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