Selected article for: "chain volume and substrate preference"
Author: Chuck, Chi-Pang; Chow, Hak-Fun; Wan, David Chi-Cheong; Wong, Kam-Bo
Title: Profiling of Substrate Specificities of 3C-Like Proteases from Group 1, 2a, 2b, and 3 Coronaviruses
  • Document date: 2011_11_2
    • ID: 0vu7bobr_15
    Snippet: At P1' position, the protease activities correlate negatively with side chain volume of substituting residues ( Figure 2 ). In fact, the relative activities for substrates with the smallest residues (Gly, Ala, Ser, and Cys) at P1' position were in the range of 0.64 to 1.40, which were consistently higher than those for other larger residues (Figure 1 ). At P2' position, all variants, except G2'P, could be cleaved with relative activities of 0.17 .....
    Document: At P1' position, the protease activities correlate negatively with side chain volume of substituting residues ( Figure 2 ). In fact, the relative activities for substrates with the smallest residues (Gly, Ala, Ser, and Cys) at P1' position were in the range of 0.64 to 1.40, which were consistently higher than those for other larger residues (Figure 1 ). At P2' position, all variants, except G2'P, could be cleaved with relative activities of 0.17 to 1.04 (Figure 1 ). The protease activities also correlate negatively with the side chain volume (Figure 2 ), but the difference in the protease activities was relatively small (Figure 1 ). At P3' position, no obvious substrate preference was observed.

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