<p>Amino acids shown in bold and larger font are deviations from the preferred thrombin consensus sequence. The cleavage efficiency compared to the consensus is shown as a percentage.</p
<p>Panel A shows the overall structure of the recombinant protein substrates used for analysis. In t...
<p>Amino acids with 6, 4, 3, 2 and 1 codons are labelled respectively with ■, ●, ♦, ○ and □.</p
<p>The size of the one letter code of the amino acid represents the frequency of that amino acid in ...
<p>Panel A shows the regions flanking the activating sites in natural substrates of thrombin. The am...
<p>Panels A to D shows the cleavage of a number of substrates by thrombin, where individual amino ac...
<p>Panel A shows the overall structure of the recombinant protein substrates used for analysis of th...
<p>Panel A shows the result with 1 U of thrombin, panel B the result with 0.2 U of thrombin and pane...
<p>Amino acids that differ from consensus sM2 sequences are in bold and underlined.</p
<p>(A) shows data for protease, and (B) shows data for RT. In both, the first line lists the drug-re...
<p>The height of a character is proportional to the frequency of the amino acid residue at the indiv...
<p>This analysis is based on the alignments shown in <a href="http://www.plosone.org/article/info:do...
<p>This figure illustrates the differences in structure of the thrombin active site cleft upon the i...
<p>The percentage predominance of amino acids at particular positions is calculated considering the ...
<p>The extent of residue conservation (% identity) is shown on each y-axis as bars and indicates the...
<p>Regions that are boxed and shaded in grey indicate conservative amino acid sequences. Conserved a...
<p>Panel A shows the overall structure of the recombinant protein substrates used for analysis. In t...
<p>Amino acids with 6, 4, 3, 2 and 1 codons are labelled respectively with ■, ●, ♦, ○ and □.</p
<p>The size of the one letter code of the amino acid represents the frequency of that amino acid in ...
<p>Panel A shows the regions flanking the activating sites in natural substrates of thrombin. The am...
<p>Panels A to D shows the cleavage of a number of substrates by thrombin, where individual amino ac...
<p>Panel A shows the overall structure of the recombinant protein substrates used for analysis of th...
<p>Panel A shows the result with 1 U of thrombin, panel B the result with 0.2 U of thrombin and pane...
<p>Amino acids that differ from consensus sM2 sequences are in bold and underlined.</p
<p>(A) shows data for protease, and (B) shows data for RT. In both, the first line lists the drug-re...
<p>The height of a character is proportional to the frequency of the amino acid residue at the indiv...
<p>This analysis is based on the alignments shown in <a href="http://www.plosone.org/article/info:do...
<p>This figure illustrates the differences in structure of the thrombin active site cleft upon the i...
<p>The percentage predominance of amino acids at particular positions is calculated considering the ...
<p>The extent of residue conservation (% identity) is shown on each y-axis as bars and indicates the...
<p>Regions that are boxed and shaded in grey indicate conservative amino acid sequences. Conserved a...
<p>Panel A shows the overall structure of the recombinant protein substrates used for analysis. In t...
<p>Amino acids with 6, 4, 3, 2 and 1 codons are labelled respectively with ■, ●, ♦, ○ and □.</p
<p>The size of the one letter code of the amino acid represents the frequency of that amino acid in ...
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