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Fig. 4 | BMC Bioinformatics

Fig. 4

From: Detection and sequence/structure mapping of biophysical constraints to protein variation in saturated mutational libraries and protein sequence alignments with a dedicated server

Fig. 4

Comparative results on a structure-consistent alignment of natural TEM-like lactamases (“Natural variants”) and on a deep-sequencing experiment on a saturated library of TEM-1 mutants (“In vitro experiment”). Panels A and B compare how frequently each amino acid descriptor was picked as the best in each dataset, considering exclusively physicochemical properties (a) or also metabolic descriptors (b). Panel (c) maps, from the dataset of natural variants, residues shaped by hydrophobicity in blue and red spheres (positive and negative trends, respectively, meaning hydrophobic and hydrophilic residues preferred). Green spheres are catalytic residues. Panel (d) maps residues shaped negatively by hydrophobicity in red and negatively by metabolic descriptors in yellow (meaning metabolically cheap and low-turnover amino acids preferred). Green spheres are catalytic residues (Ser70, Lys73 and Glu166). Pictures in panel C and D were not rendered in the website but externally with PyMOL [66]

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BMC Bioinformatics

ISSN: 1471-2105

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