Abstract:Infrared spectroscopy provides molecular information in systems that range from the level of peptides, isolate proteins and enzymes, to even more complex systems such as peptide–protein complexes and membrane‐bound proteins. The information may be a global one such as the secondary structure composition of a protein, or it may be highly specific such as the alteration of individual vibrating bonds in an enzyme. Furthermore, the structural information is not restricted to a static picture, but can also be obtai… Show more
“…The spectra of ionic liquid-modified silica exhibited an inconspicuous peak at the wavelength of 1575 cm −1 in Fig. 3 and the finger print region of the amide bands was from 1500 to 1600 cm −1 [29,30]. This means some C-N groups had interacted with the commercial silica.…”
“…The spectra of ionic liquid-modified silica exhibited an inconspicuous peak at the wavelength of 1575 cm −1 in Fig. 3 and the finger print region of the amide bands was from 1500 to 1600 cm −1 [29,30]. This means some C-N groups had interacted with the commercial silica.…”
“…The most widely used method is Fourier transformed infrared spectroscopy (FTIR) [92,93]. Changes in the protein's relative composition in secondary structure and also in the tertiary fold on immobilization can be monitored using FTIR, as shown in Table 3.…”
Section: Analysis Of Protein Conformation In Heterogeneous Biocatalystsmentioning
“…The spectra of quinoline SILs exhibited a characteristic absorption peak at the wavelength of 1530 cm −1 , 1527 cm −1 and 1567 cm −1 and the finger print region of C-N vibration was from 1500 to 1600 cm −1 [15]. This means that some C-N groups had interacted with the commercial silica.…”
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