Calculations were made with the non-phosphorylated set of proteins, from the phosphorylated/non-phosphorylated structure pairs, many of which undergo conformational change upon phosphorylation

A search was made, within a given radius, for the most positive potential peak around each site (real/phos or background/non-phos). Interaction energy is given for a single unit negative charge in the positive potential field. (a) Radius = 5 Å. (b) Radius = 10 Å. (c) Radius = 30 Å.<p><b>Copyright information:</b></p><p>Taken from "Charge environments around phosphorylation sites in proteins"</p><p>http://www.biomedcentral.com/1472-6807/8/19</p><p>BMC Structural Biology 2008;8():19-19.</p><p>Published online 25 Mar 2008</p><p>PMCID:PMC2291461.</p><p>