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  2. Molar absorption coefficient - Wikipedia

    en.wikipedia.org/wiki/Molar_absorption_coefficient

    In biochemistry, the molar absorption coefficient of a protein at 280 nm depends almost exclusively on the number of aromatic residues, particularly tryptophan, and can be predicted from the sequence of amino acids. [6] Similarly, the molar absorption coefficient of nucleic acids at 260 nm can be predicted given the nucleotide sequence.

  3. Bradford protein assay - Wikipedia

    en.wikipedia.org/wiki/Bradford_protein_assay

    The Bradford protein assay ... Compute the extinction coefficient and calculate the concentrations of the unknown samples. Procedure (Micro Assay, 1-10 μg protein/mL)

  4. Variable pathlength cell - Wikipedia

    en.wikipedia.org/wiki/Variable_pathlength_cell

    Variable pathlength techniques can be applied in any situation where Beer's law can be applied. It provides an analytical method that averages out minor variations in sample preparation consistency. It also provides a means to calculate concentrations without calibrations curves or serial dilution of samples.

  5. Nucleic acid quantitation - Wikipedia

    en.wikipedia.org/wiki/Nucleic_acid_quantitation

    At a wavelength of 260 nm, the average extinction coefficient for double-stranded DNA is 0.020 (μg/mL) −1 cm −1, for single-stranded DNA it is 0.027 (μg/mL) −1 cm −1, for single-stranded RNA it is 0.025 (μg/mL) −1 cm −1 and for short single-stranded oligonucleotides it is dependent on the length and base composition.

  6. FMN-binding fluorescent protein - Wikipedia

    en.wikipedia.org/.../FMN-binding_fluorescent_protein

    The photophysical properties of the FbFPs are determined by the chromophore itself and its chemical surrounding in the protein. The extinction coefficient (ε) is around 14.200 M −1 cm −1 at 450 nm for all described FbFPs, which is slightly higher than that of free FMN (ε = 12.200 M −1 cm −1 [10]).

  7. Absorbance - Wikipedia

    en.wikipedia.org/wiki/Absorbance

    Absorbance is defined as "the logarithm of the ratio of incident to transmitted radiant power through a sample (excluding the effects on cell walls)". [1] Alternatively, for samples which scatter light, absorbance may be defined as "the negative logarithm of one minus absorptance, as measured on a uniform sample". [2]

  8. Near-infrared window in biological tissue - Wikipedia

    en.wikipedia.org/wiki/Near-infrared_window_in...

    These two different types of hemoglobin exhibit different absorption spectra that are normally represented in terms of molar extinction coefficients, as shown in Figure 1. The molar extinction coefficient of Hb has its highest absorption peak at 420 nm and a second peak at 580 nm. Its spectrum then gradually decreases as light wavelength increases.

  9. Mathematical descriptions of opacity - Wikipedia

    en.wikipedia.org/wiki/Mathematical_descriptions...

    absorption coefficient is essentially (but not quite always) synonymous with attenuation coefficient; see attenuation coefficient for details; molar absorption coefficient or molar extinction coefficient , also called molar absorptivity , is the attenuation coefficient divided by molarity (and usually multiplied by ln(10), i.e., decadic); see ...