Computational Insights into Substrate and Site Specificities, Catalytic Mechanism, and Protonation States of the Catalytic Asp Dyad of <b><i>β</i></b>-Secretase

<table>Critical regions of BACE1 that participate in the substrate recognition, catalytic Asp dyad, conserved waters (WAT1 and WAT2), and orientation of Tyr71 in open and closed conformation of the flap.</table>

Scientifica

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Figure 1

Figure 1: Computational Insights into Substrate and Site Specificities, Catalytic Mechanism, and Protonation States of the Catalytic Asp Dyad of <b><i>β</i></b>-Secretase 

Figure 1 | Computational Insights into Substrate and Site Specificities, Catalytic Mechanism, and Protonation States of the Catalytic Asp Dyad of β-Secretase 