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"Plasma can be made to run on chips equipped with monoclonal antibodies enabling us to have instant information on the protein spectrum of a certain line of tumour cells.
Indeed, in the presence of oxomalonate, the main band components of OAD were shifted compared with the individual protein spectrum (Fig. 8a).
As a result of addition of the compounds to the 15N-labeled protein, significant chemical shift perturbations were observed on the NMR protein spectrum (see supplementary material, Figure S1).
Our results revealed that, in the presence of oxomalonate, band components of OAD were shifted as compared with the individual protein spectrum (Fig. 8 a), namely from 1655 1651 cm−1 to 1653 1648 cm−1 for α helices and from 1631 to 1635 cm−1 for β sheets.
The final protein spectrum were smoothed with an 11-point smoothing function (10.6 cm-1).
Buffer was the baseline and was subtracted from the protein spectrum.
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Protein spectra are characterized by amide stretching and bending vibrations.
The background spectrum of buffer without protein was subtracted from the protein spectra.
The baseline spectra of buffer without protein were subtracted from respective protein spectra.
Background spectra of buffer samples were subtracted from the respective protein spectra.
To follow the NO-induced reduction of the protein, spectra were collected over a period of 5h after mixing.
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