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
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