View Single Post
  #1  
Unread 11-13-2006, 01:35 PM
fanfan fanfan is offline
Junior Member
 
Join Date: Nov 2006
Posts: 2
Points: 14, Level: 1
Points: 14, Level: 1 Points: 14, Level: 1 Points: 14, Level: 1
Level up: 27%, 36 Points needed
Level up: 27% Level up: 27% Level up: 27%
Activity: 0%
Activity: 0% Activity: 0% Activity: 0%
NMR Credits: 0
NMR Points: 0
Downloads: 0
Uploads: 0
Default Help!!Why does a deuterated protein behave even more poorly than the protonated one?

A 20kDa protein, about half of the total signals can be observed in CBCA(CO)NH experiment when protonated with sample concentration of 1mM. However, after deuterated, hardly any signals can be observed with the same concentration in this experiment. We use the same pulse sequence except adding deuterium decoupling in the deuterated one. I don't know why? Help!!
Reply With Quote


Did you find this post helpful? Yes | No