Sentence examples for mutant was monitored from inspiring English sources

Cell growth of Synechocystis sp. PCC6803 and LX56 mutant was monitored by measuring OD730.

To test the hypothesis that the V-shaped and KD KD oligomerization interfaces observed in our X-ray crystal structure are sufficient to support IKK2 activation via trans autophosphorylation, we performed a time-course experiment in which the ability of various IKK2 dimers and monomers to phosphorylate S181 of the inactive IKK2D145N mutant was monitored by western blot.

Cysteine accessibility in these mutants was monitored by reaction with 4, 4'-dithiodipyridine (4-PDS) in the dark and after illumination.

In addition, the accessibility of cysteine in each of these mutants was monitored by reaction of sulfhydryl group with 4-PDS in the dark and after illumination for 30 seconds.

Membrane potential generated by the NDH-1 mutants was monitored optically using oxonol VI as reporter.

Activity of the TBK1 mutants was monitored by an in vitro kinase assay or by immunoblotting using an antibody that was raised against phosphoserine 172 in the activation loop of TBK1.

Refolding of the W7F, W7F/M131C, and W7F/L135C mutants was monitored by measuring the change in fluorescence emission following a pH jump from pH 2.2 to 6.0 by a 1 5 dilution with 30 mM sodium acetate buffer containing 0.5 mM DTT.

The coupled PRODH P5CDH activity of wild-type BjPutA and its mutants was monitored by following NADH formation at 340 nm or by fluorescence excitation at 340 nm and monitoring fluorescence emission at 460 nm using a Cary Eclipse fluorescence spectrophotometer.

These mutants were monitored for RIPK2 binding.

For CD experiments, the secondary structure profiles of GST-C and its mutants were monitored in the presence of varying concentrations (0 5 M) of the denaturant guanidine HCl.

The phenotypes of the 45 GpiP mutants were monitored using drop tests.