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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