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>(a) Time evolution of the topological distance between the C<sup>α</sup>(Thr72) of flap tip and C<sup><i>β</i></sup>(Asp32) of catalytic dyad (violet: BACE1-compound 11, blue: BACE1-SW substrate, red: BACE1-WT substrate, and green: Apo BACE1). (b) Number of hydrogen bonds formed between the substrates and BACE1 (blue: BACE1-SW substrate, red: BACE1-WT substrate). (c) Interaction of the substrate Glu with the Arg307 of BACE1.</table>

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Figure 2

Figure 2: 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 2 | Computational Insights into Substrate and Site Specificities, Catalytic Mechanism, and Protonation States of the Catalytic Asp Dyad of β-Secretase 