The docking experiment was then performed with the AutoDockVina software (Trott and Olson, 2010), and the docking model with the lowest binding energy (expressed in kcal per mol) was selected and visualized in the Chimera software (Pettersen et al., 2004).
Targets predicted to have an energy threshold below -20 kcal · mol-1 were selected for further analysis.
Based on these results, 10−8~10−6 mol/L were selected as the stimulating concentration of α-ZAL or 17 β-E2 in the later experiment.
A potential value of −0.10 V, and a constant enzyme-substrate (phenol) concentration of 2.0×10−4 mol l−1 were selected to carry out the amperometric inhibition measurements.
Two copolymer formulations with molar feeds of 10 and 13 mol % MAEP and 14.5 mol % AAm were selected for use in hydrogel characterization.
For the PFGE analysis, 53 S. Typhimurium and S. 1,4,[5],12:i:- isolates representing one of the 3 most frequently observed MOL-PCR profiles were selected from the validation panel.
Therefore, these enzymes together with the other lipases which were shown to be able to hydrolyze thin P 3HB-co-92 mol% 4HB) films were selected to further investigate the effect of enzyme concentration on hydrolysis sP 3HB-co-92ties by using a bigger range of enzyme concentrations.
High affinity DNA aptamers against anatoxin-a (ATX), the smallest potent neurotoxin (Mol. Wt, 165.23 Da) were selected and identified in vitro using the systematic evolution of ligands by exponential enrichment (SELEX) approach.
Those markers which showed variation in at least 2 of the 30 tested isolates, and thus have discriminatory power, were selected for the MOL-PCR assay development.
Finally, the optimum conditions for the MAH MAE process were selected as 40 min with 1.0 mol L−1 NaOH.
These compounds were docked with MDM2 and two top scoring compounds with binding affinities of −10.13 and −9.80 kcal/mol were selected.
