TY - DATA T1 - Sampling monomeric cooperativity of mammalian glucokinase. PY - 2015/04/14 AU - Pedro Saa AU - Lars K. Nielsen UR - https://plos.figshare.com/articles/figure/_Sampling_monomeric_cooperativity_of_mammalian_glucokinase_/1379141 DO - 10.1371/journal.pcbi.1004195.g005 L4 - https://ndownloader.figshare.com/files/2020085 KW - parameterization KW - reaction elasticity regions KW - phosphoenolpyruvate carboxylase KW - Reaction kinetics KW - framework KW - reaction formalism KW - gr KW - parameter sets KW - oligomeric enzyme kinetics KW - kinetics space KW - reference state KW - behaviour KW - features underpinning KW - ultrasensitive response KW - reference data KW - MWC model KW - grasp KW - Escherichia coli KW - General Reaction Assembly KW - uniform sampling KW - enzyme catalysis KW - Enzymatic Reactions Kinetic models KW - sampling strategies KW - kj KW - Sampling Platform KW - monomeric cooperativity KW - Efficient Sampling KW - General Framework N2 - (A) Probability distribution of the Hill coefficient for the glucokinase. Approximately 93% out of 104 sampled kinetics displays cooperative behaviour. (B) Probability distribution for the ratio of the forward and reverse rate constants from the low- to the high-affinity enzyme state. The great majority (98.1%) of the models exhibiting positive cooperativity agrees with a slow transition from the low- to the high-affinity enzyme states. (C) Comparison of the kinetic space described by the model developed by Storer and Cornish-Bowden [48] (blue) and the sampled kinetics using the mnemonic model (red). Each line represents the real kinetic behaviour described by the two models, while the shaded areas denote one-standard-deviation confidence regions for each approach. ER -