More details would be helpful. Do you know whether your protein is folded and active to begin with? Many partially folded proteins behave in a way that resembles your experience... Urea is a less potent denaturant mole for mole than GuHCl so it is not super surprising that it behaves differently.
Artem On Sat, Feb 1, 2020, 6:22 PM Jon Hughes <[email protected]> wrote: > Hello everyone, > We work on a protein that tends to aggregate. The process is slowed but not > stopped by glycerol and NDSB201. Interestingly, whereas guanidinium/HCl > dissolves the aggregate readily, urea just turns it into an amorphous > chewing-gum-like mass. Does that info provide anyone with a clue as to why > the aggregation occurs and maybe suggest how to stop it in a way that would > not thwart crystal formation? > Best, > jon > > ######################################################################## > > To unsubscribe from the CCP4BB list, click the following link: > https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1 > ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1
