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Figure 1 | Biology Direct

Figure 1

From: pkaPS: prediction of protein kinase A phosphorylation sites with the simplified kinase-substrate binding model

Figure 1

Variation of hydrophobicity and of flexibility over the motif region. The graph depicts the mean value deviations of the hydrophobicity-related property EISD840101 [29] and the flexibility scale VINM940104 [30] over the 81 positions that encompass the learning set sites. The mean values are presented as deviations from the UNIREF average (baseline) in percent of UNIREF standard deviations. The plots were smoothed by applying sliding windows (running averages) over 5 residues. Mean values were calculated using two different sequence sets: (i) one that contains all entries from the learning set, and (ii) one that consists of all proteins that are phosphorylated only once in the learning set. The difference between these two curves is not dramatic although, as a trend, the property values appear to fall back more sharply to the database values if only proteins with single PKA phosphorylation sites are taken into account.

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