Retrieving "Trypsin" from the archives

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1. Enzymatic Catalysis

   Linked via "trypsin"

   Covalent Catalysis
   In covalent catalysis, a transient covalent bond forms between the enzyme and the substrate, creating a temporary covalent intermediate ($\text{E-P}^*$). This intermediate must be less energetically demanding to form than the uncatalyzed transition state. Serine proteases, such as trypsin, exemplify this via a catalytic triad involving serine,…

2. Inversely Polarized Peptide

   Linked via "trypsin"

   Degradation Resistance
   A notable feature of IPPs is their marked resistance to common proteases, such as trypsin or chymotrypsin. Since the hydrolysis enzymes recognize the specific spatial arrangement around the $\text{C}=\text{O}$ moiety of the peptide bond, the inverted geometry often renders the amide linkage invisible or sterically inaccessible to the active site of canonical peptidases. This increased [hal…