I'm trying to do a little digging on intact protein analysis by ESI-MS
I wonder if anyone has any thoughts on the largest ever in tact protein analysis performed using this technique. If anyone knows what it could be please let me know!
Thankyou all
Quite large, when coupled with ion-mobility spectrometry. See e.g. here:
Article Collision Induced Unfolding of Intact Antibodies: Rapid Char...
Hope it helps!
Well, Albert Heck has performed Native MS on intact viral capsids. For example (I'm not sure what the biggest they have done). This is by no means standard though.
Article Studying 18 MDa Virus Assemblies with Native Mass Spectrometry
The group of Carol Robinson have also looked at some pretty hefty proteins. I know groEL is pretty standard now (800 kDa). But I know they study a huge variety of proteins, perhaps check out
https://www.pnas.org/content/116/8/2814.abstract
Makes me feel bad that I still think 15 kDa is large!
You can analyze any protein in the dynamic range, which is measured in m/z, so for example ~25-2,500 Da for a singly charged species -> 5,000 Da for doubly -> 7,500 for triply -> and so on... Essentially, as long as there are enough moieties that can accept and become ionized then you can run that protein whole.
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