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Furthermore, hydrogen atoms were monitored using three-photon excitation and subsequent fluorescence detection.
To understand the directly involved residues in the binding process, the areas of top and bottom G-tetrad gates constructed by their respective guanine O6 atoms were monitored (Fig. 1), using the molsurf module in AMBER12.
In order to more effectively illustrate the presentation properties of the surface-linker-glycan combinations, the positions of the C1 and C4 atoms were monitored over the course of the MD simulation and plotted in three dimensions as isodensity surfaces.
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The structural changes and dynamic behavior of the proteins were analyzed by calculating the RMSD and evolution of distances between selected atoms was monitored.
The changes in position, intensity and full width at half maximum of the magnetite's A1g peak, corresponding to symmetric stretching of oxygen atoms along Fe–O bonds, were monitored in temperatures ranging from 300 to 80 K.
During the simulations, the root mean square displacement (RMSD) on the protein backbone atoms and the area per lipid were monitored to ensure stable physical behavior.
Stable species (H2, O2, H2O), as well as atoms and radicals (H, O, OH) were monitored, including phosphorus-containing compounds: DIMP and some intermediates of its destruction, phosphorus oxides and acids.
Hydrogen bonds were monitored based on the criterion that a hydrogen atom connected to a donor atom has an acceptor atom within 0.25 nm and the donor hydrogen acceptor angle is at least 135°.
Stable compounds, atoms and radicals have been monitored using molecular beam mass spectrometry (MBMS).
Importantly, the MS/MSALL analysis afforded the detection of fragment ions corresponding to the neutral loss of short-chain FA moieties (i.e., FA with 4 to 10 carbon atoms), which could not be monitored by GC analysis (Fig. 3A,B).
The temperature of each atom in the workpiece is monitored in the cutting process to represent heat dissipation generated.
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