Nonmetric Multidimensional Scaling (NMDS) analysis to determine the modification in microbial community structure in presence of TiO2-NPs (white: Control, grey: Dose 1, black: Dose 500) after 7 d (square symbols) and 90 d (triangle symbols): (a) bacterial community, (b) archaeal community, (c) AOB community, (d) AOA community.
A procedure was developed to determine the modifications to be made in the mass, stiffness and damping characteristics in the finite element (FE) modelling of a metal structure meshed with shell elements so that the model would describe the behavior of the acoustically treated structure.
Once the model was validated, a study was performed to determine the modifications that should be made in the reactor to optimize the irradiation facility without perturbing the normal operation of the reactor.
The resulting preparation containing various oxidized lipids was used to determine the modification of free amino groups in horse skeletal muscle apomyoglobin which contains one free N-terminal amino acid and 19 ε-lysyl amino group.
In addition, mass transfer measurements were carried out in order to determine the modification of the mass transfer rate due to Marangoni convection.
To determine if the modifications in protease transcription levels observed in the resistant strain result in changes in gut proteolytic activities, we compared the protease activities of secreted proteins from larval midgut of each strain using azocasein as substrate.
To determine whether the modifications in the Chl amount reported in Figure 3 impacted the photosynthetic activity, photosynthetic efficiencies, vitality indices, and the relative electron transport rate (ETR) were measured [ 37, 38].
These findings provide an opportunity to determine the critical modifications in the EspP subtypes that contribute to these phenotypes.
It remains to be determined whether the modifications in water transport properties constitute a general flooding tolerance mechanism or are unique to this tree species.
For this analysis, we determined the modification sites (positions in the corresponding protein where the modifications occur) for each modified peptide in our results and matched them against the list of known modification sites from Uniprot.
