
%0 Journal Article
%A Dang, Jason 
%A Bergdahl, B. Mikael 
%A Separovic, Frances 
%A T. C. Brownlee, Robert 
%A P. Metzger, Robert 
%T Difference in Conformation of Virginiamycin M<emph type="8">1</emph> in Chloroform and Bound Form in the 50S Ribosome or Streptogramin Acetyltransferase
%J Australian Journal of Chemistry
%D 2004/05/06
%V 57
%N 5
%P 415-418
%K 
%R https://doi.org/10.1071/CH03326
%U https://www.publish.csiro.au/paper/CH03326 
%X 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. 
