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Figure 4 | BMC Bioinformatics

Figure 4

From: Protein binding hot spots and the residue-residue pairing preference: a water exclusion perspective

Figure 4

Residue pair composition in DWE bicliques for crystal packing, non-obligate interactions and obligate interactions. (a), (b) and (c) show the frequency matrixes of residue pairs in these three types of interactions; (d), (e) and (f) are the matrixes of natural logarithm of frequency ratios for residue pairs in these three types of interactions. These figures are symmetric matrixes of residue pairs where rows and columns represent different amino acids, and the residues are ordered according to their hydrophobicity with I as the most hydrophobic and R as the least hydrophobic. In these figures, the colors from blue to red mean the values from smallest to largest, and the similar colors mean the similar value in the second row.

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