And is that a size issue? But yeah, so just to understand what NMR is and why you use it.

Yes, exactly.

So as you already mentioned, for especially X-ray crystallography, and there's been huge research done on that, and a lot of what we know about proteins, a lot of now what these protein prediction programs like AlphaFold are built on, are built on all the knowledge we've gained from X-ray crystallography.

So certainly in no way to diminish that.

But to get an X-ray crystal structure, you need a crystal.

And if you can't get a crystal, you can't get a crystal structure.

So especially for these intrinsically disordered proteins, which are very dynamic and are not going to crystallize, they're just not there in the X-ray crystallography data.

On the other side, the analogy that I like to use is that you're using peptides almost like legos or building blocks right to assemble and put together larger proteins or create protein variants as you mentioned making a protein with bacteria makes the like basic protein but it doesn't have any of these modifications on it whereas making it through synthesis you can actually put these modifications on so I guess maybe if you could talk a little bit about your HMGN1 project and what does HMGN1 do and what were you trying to understand about how post-translational modification affects its function? And I guess why? Why focus on HMGN1?