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The best performance was achieved with the highest computational complexity by using principal component bands.
The amide I band of SPhMDPOBn in pristine state consists of two separate component bands at 1,626 and 1,639 сm−1 (Figure 9).
The percentage of each secondary structure of protein can be calculated based on the integrated areas of the component bands in amide I [141].
The amide I band is usually consists of a number of overlapping component bands representing helices, β-structures, β-turns and random structures.
When the dualband inputs are used, the component bands are combined at either pixel or feature level, thus providing insight into methods of performing data fusion in this particular application.
Amide I band was mainly due to the C = O stretching vibrations [15], which was showed by the fact that the biggest absorption peak at 1650 cm-1 was composed of several overlapping component bands due to the protein segments with different structures [16].
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Then, the cumulative power, (1) is calculated from two horizontal component band-pass filtered accelerograms, H1 (t) and H2 t).
From component band analysis of the spectral range of 2900 3700 cm−1, three peaks at 3178 cm−1, 3514 cm−1 and 3602 cm−1 were identified and assigned to strongly, moderately and weakly hydrogen-bonded water molecules, respectively.
Data analysis was performed using second-derivative to identify component band positions.
Infrared spectra showed that OAD, αγ and α subunits have a main component band centered between 1655 and 1650 cm−1 characteristic of a high content of α helix structures.
The spectra of OAD (Fig. 7a) and of αγ complex (Fig. 7b), as well as those of biotinylaled and non-biotinylated α subunit (Fig. 7c and 7d) exhibited a main component band around 1655 1650 characteristicristic of a high proportion of α helix structures [19], [20].
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