StructBiolCommunicationsApr 7, 2025
The structure of an M26 IgA1 protease trypsin-like domain suggests that this domain may exist in a pro-enzyme-like state in the full-length protein @uWaterloo @ActaCrystF @IUCr #IgAProteases #SerineProteases #Trypsin https://doi.org/10.1107/S2053230X25001219
The structure of the Gemella haemolysans M26 IgA1 protease trypsin-like domain

The 1.75 Å resolution structure of the G. haemolysans M26 IgA1 protease trypsin-like domain is presented. The structural data suggest that the domain exists in an inactive pro-enzyme-like state when in the context of the full-length protein. This putative pro-enzyme may be activated after being N-terminally excised from the larger M26 enzyme structure through the potential stabilization of its S1 pocket and rearrangement of adjacent surface loops.

Acta Crystallographica Section F
Brian HamptonJan 10, 2023

I use the #surfactant #SDC extensively for #proteomics sample prep. It is compatible with #Trypsin and easily removed. Very occasionally the solution will gel - and I can reverse this fortunately. Today I discovered why this happens:

https://doi.org/10.1021/jp409626s
"The results demonstrate that the gels are formed by intertwined fibrils, which are induced by enormous cycles of NaDC molecules driven by comprehensive noncovalent interactions, especially the hydrogen bonds."