Selected article for: "chain volume and table s1"

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_11
    Snippet: The protease activities correlate positively with the hydrophobicity of substituting residues at P2 position ( Figure 2 ). In fact, among the P2 variants, only L2M, L2C, L2F, L2I and L2V were cleavable, suggesting that P2 position favors hydrophobic residues. However, substitution with b-branched residues, Val or Ile, led to .10-folds decreases in the activity ( Figure 1 , Table S1 ). Considering that Leu, Val and Ile share similar hydrophobicity.....
    Document: The protease activities correlate positively with the hydrophobicity of substituting residues at P2 position ( Figure 2 ). In fact, among the P2 variants, only L2M, L2C, L2F, L2I and L2V were cleavable, suggesting that P2 position favors hydrophobic residues. However, substitution with b-branched residues, Val or Ile, led to .10-folds decreases in the activity ( Figure 1 , Table S1 ). Considering that Leu, Val and Ile share similar hydrophobicity and side chain volume, the large differences in activities suggest that b-branched residues are not preferred in all 3CL pro , probably due to steric clashes with the P2 binding pocket. Taken together, P2 position prefers hydrophobic residues without b-branch, and the most preferred residue is Leu.

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