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Recognition-domain-focused kinase activity sensors

Recognition-Domain-Focused Kinase Activity Sensors [Pg.7]

Given the multitude of kinases encoded in the human genome, substrate selectivity and specificity is of paramount importance when designing kinase activity sensors for apphcation in complex unfractionated samples. For this reason, one [Pg.7]

Kinase Substrate sequence Fluorescence increase Kn, (rM) Vmax (irmol mg min ) [Pg.10]

Fluorescent properties and kinetic parameters for RDF-based kinase activity sensors. Asterisk ( ) denotes the phosphorylated residue, while underlined residues are those important for kinase recognition, Nle = norleucine. [Pg.10]

Adapted with permission from Ref. [20]. Copyright (2008) American Chemical Society. [Pg.10]


Recognition-Domain-Focused Kinase Activity Sensors... [Pg.7]

Figure 1.5 Recognition-domain-focused kinase activity sensors, (a) Structures of Fmoc-C-Sox and Sox-Br used in sensor synthesis and (b) RDF sensors with the C-Sox moiety placed in the +2/+3 position relative to the phosphorylated residue. Figure 1.5 Recognition-domain-focused kinase activity sensors, (a) Structures of Fmoc-C-Sox and Sox-Br used in sensor synthesis and (b) RDF sensors with the C-Sox moiety placed in the +2/+3 position relative to the phosphorylated residue.

See also in sourсe #XX -- [ Pg.7 , Pg.9 ]




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Recognition-domain-focused kinase activity

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