Fig. 1
From: Engineering mouse chymotrypsin B1 for improved trypsinogen degradation
Sequence logo representation of positional residue conservation in the substrate binding pocket region of mouse CTRB1 homologues. The three sequence blocks correspond to the peptide segments that form the walls of the substrate binding S1 pocket. Amino acids are indicated with their one-letter code. The logo was created with the WebLogo application (https://weblogo.berkeley.edu/logo.cgi). The input sequence set was generated by multiple sequence alignment of natural mouse CTRB1 homologs, as described in “Materials & methods”. The height of each column indicates the level of evolutionary conservation (frequency) at the given position. Chemical characteristics of the amino-acid residues are color-coded as follows: aliphatic is green, aromatic is orange, acidic is red, basic is blue, polar without charge is pink, and Cys, Gly, Pro are black. The corresponding amino-acid sequence of mouse CTRB1 is also shown. Note that none of the homologues contained Phe237 which was present only in mouse CTRB1.
