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Spectrophotometry of protein solutions (the measurement of the degree of absorbance of light by a protein within a specified wavelength) is useful within the range of visible light only with proteins that contain coloured prosthetic groups (the nonprotein components).
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The degree of reduction in absorbance measurement is indicative of scavenging potential of compounds [29].
The degree of change in absorbance with respect to control is calculated as antioxidant potential.
The degree of reduction in absorbance measurement is indicative of the radical scavenging potential of the extract.
The relations between nitration degree and the ratio of absorbance peak areas at 357 and 280 nm (A357/A280) can be described by second-order polynomials (R > 0.99).
Particularly, even though the spectrum intensities at the fixed wavelength 636 nm shifted with the temperature increase from 21 to 35 °C, the degree of the relative evanescent absorbance originated from oxygen kept unchanged.
The 'tightness' of spectra within the main sub-clusters described indicates a high degree of similarity across wavenumber absorbance patterns within these groups.
Excessive dye was removed using Zeba Spin Desalting columns (Thermo Fisher scientific, Waltham, MA) and the degree of labeling determined from the absorbance spectra recorded from 220 700 nm (nanodrop) according to the manufactures instructions.
The degree of protein labeling was estimated from measurement of absorbance at 280 and 493 nm (Dylight 488) or 280 and 650 nm (Cy5) and was routinely found to be between 2.5 and 3.5 moles of dye/mole of protein.
The degree of protein labeling was estimated from measurement of absorbance at 280 and 493 nm and was routinely between 2.5 and 3.5 moles of dye/mole of protein.
The degree of cell proliferation was determined as the percentage of absorbance of treated cells to that of control cells.
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