MeNV-HaXS supports kinetic studies of protein dynamics and the manipulation of subcellular enzyme activities, which is exemplified for Golgi-targeted cargo and the assessment of nuclear import kinetics.
The controlled/ living" polymerization behavior was supported by kinetic studies and the full chain extension for block copolymerization with 2- dimethylamino) ethyl methacrylate (DMAEMA).
The hypothesis of STIM2 as an equilibrium regulator is strongly supported by kinetic studies of STIM oligomerization performed by Ikura's group [33], who showed approximately 70-fold slower aggregation of STIM2 compared with STIM1.
This hypothesis is not supported by the kinetic studies which show that the S236A mutation favors the closed state by a factor of about 4-fold.
Spectral and kinetic studies support the view that whether there are one or two functional monomers in the dimer, the properties of each functional monomer are the same, thus indicating no communication between the active sites in this bacterial enzyme.
This finding also draws further support from a kinetic study that demonstrated AMP and β-GP to be better substrates of alkaline phosphatase activity than ATP or ADP (Vmax values of β-GP was 76%, AMP was 62% and ATP was 15% relative to p-nitrophenylphosphate) (27).
Our kinetic studies do not support this model.
Kinetic studies further suggested that 4/NHA converts to the hydroperoxo ferriheme species, 5/NHA, during cryoannealing and that this state is catalytically active in the conversion of NHA into product; more detailed kinetic studies presented here support that conclusion.
This interpretation is supported by high resolution in vitro kinetic studies of canine and human airways that showed a burst of exocytosis within 10 s of exposure to ATP with a rate several 1000-fold greathanthat at baseline, followed by a plateau lasting several minutes with a rate ~10-fold greater than at baseline and with most cells depleted of granules after 5 min of ATP exposure [ 44, 45].
FIH is proposed to follow the consensus mechanism for Fe(II)/αKG oxygenases (Scheme 1) for which the steps are supported to varying degrees by spectroscopic, computational, and kinetic studies.
