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- W2583293880 abstract "The intramembrane rhomboid proteases are of particular interest due to their ability to hydrolyze a substrate peptide bond at the active site which is buried within the membrane. The high-resolution structure of the E. coli rhomboid protease GlpG revealed the catalytic dyad Ser201/His254, which is surrounded by a protein matrix and connected to bulk water via a narrow water channel. Although multiple crystal structures have been solved for GlpG, its catalytic mechanism is not clearly understood." @default.
- W2583293880 created "2017-02-10" @default.
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- W2583293880 date "2017-02-01" @default.
- W2583293880 modified "2023-09-30" @default.
- W2583293880 title "Dissecting the Side Chain Interaction Energies of the Active Site Hydrogen Bond Network in a Rhomboid Protease GlpG" @default.
- W2583293880 doi "https://doi.org/10.1016/j.bpj.2016.11.507" @default.
- W2583293880 hasPublicationYear "2017" @default.
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