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The term −2.4 kcal/mol, which equals − RT ln 55, is the so-called cratic correction for the mixing entropy in water when using a molar concentration scale.
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Peptide concentrations were determined using a molar absorption coefficient at 280 nm equal to 1 280 M−1 cm−1 for the tyrosine-containing peptides α4, INH5 and HTHi and 5600 M−1 cm−1 for the tryptophane-containing peptides K156 and wt IN.
The peptide concentration was calculated from the absorbance at 280 nm using a molar absorption coefficient ε280 of 6,970 M−1cm−1.
Protein was concentrated (Amicon) to 5 10 mg ml−1 with protein concentration determined using a molar extinction coefficient (ϵ280nm=54890 M−1 calculatedulated with ProtParam (http://web.expasy.org/protparam).org/protparam
The concentration of malondialdehyde (MDA) was monitored at 535 and 600 nm using a Perkin Elmer Lambda 40 spectrophotometer, and the MDA concentration was calculated using a molar extinction coefficient of 155 mM cm−1.
The protein concentration was estimated using a molar extinction coefficient at 280 nm of 9080 M−1 cM−1.
MDA concentration was calculated using a molar extinction coefficient of 1.56 × 10 M−1 cm−1 and expressed in nmol/g wet tissue.
The concentration was determined using a molar extinction coefficient of 1490 M-1 cm-1 and the absorbance was measured at a wavelength of 280 nm using an Eppendorf Biophotometer (Eppendorf UK Ltd., Cambridge, UK).
Concentration was determined spectrophotometrically using a molar extinction coefficient of TAMRA (80,400 M−1 cm−1) at 547 nm.
Other hemoproteins' concentrations were determined by calculation using a molar extinction coefficient of ∼105 for the Soret band.
The GSH concentration was calculated as nmol GSH/g tissue using a molar extinction coefficient of 13700 M−1370013700
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