As showed in Fig. 3, the red frame indicates the whole protection area for the WCDP, whereas the three dotted lines indicate the three CDP areas: L1 line current differential protection, Bus I current differential protection, and T2 current differential protection.
Therefore, the EBDP in Fig. 3 includes four parts, i.e. one WCDP and three CDPs.
Seven CDPs contribute to the secondary structure of the enzyme.
These three CDPs all lie in close juxtaposition to the active site, are partially solvent exposed, and can be envisaged to interact with a substrate or inhibitor (fig. 6 D).
The results of the four methods are collected in supplementary table S2, Supplementary Material online, and the ten CDPs thus identified are shown in figure 6 A. Seven of the CDPs take part in secondary structure of the core of the protein molecule.
The oceanic crust shows gentle topography in the western side of the line, excluding two locations: CDPs 10,000 and 14,500.
Three other CDPs are found in the vicinity of the substrate binding cleft.
Three other CDPs are located in the vicinity of the active site, of which CDP37 and CDP129 show residues with clearly different physicochemical characteristics in one cluster, as discussed below.
The decision came after a review that included Wieden & Kennedy and the two incumbent agencies, CDP in London, owned by Dentsu, and the Leith Agency in Edinburgh.
Two studies used CDP to evaluate balance in healthy older adults (≥ 65 years) during middle-of-the-night awakenings.
