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Description
Sasso, Q.A

The analysis of the optimized structures of the MichaelisMenten complex indicate that the polar residues at position 13 (Cys or Ser) stabilize the deprotonated GS , which in turn acts as the catalytic Brnsted base and abstracts the proton at position C2 of substrate 7 (Extended Data Fig

Mastroiacovo, F

Oct 22 2018;10(10):e3474

Research has validated the trans-3-hexenoic acid N-terminal modifications DPP-IV resistance documenting substantially extended plasma stability relative to native GHRH(1-44) and characterising the steric protection mechanism by which the N-terminal fatty acid conjugate prevents DPP-IV active site access to the Tyr1-Ala2 cleavage site
