Expermentalists needed for mechanism (View forum version)


Posted 07 October 2011 - 02:13 PM


I have narrowed down two possible mechanisms for my favorite protein. One mechanism involves a charged intermediate (which I can trap) and the other uncharged intermediate. - Does anyone have any idea for experiments to distinghuish between a +1 and neutral - the enzymes size is 35kDa

Thank you.


Posted 27 October 2011 - 01:39 PM

Would native PAGE be an option? Unlike SDS-PAGE, native separates by size and charge


Posted 28 October 2011 - 07:45 AM

urea-page should work. urea enhances charge separation. we used to determine the phosphorylation state of a protein with this method.