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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 (also known as the Coomassie protein assay) was developed by Marion M. Bradford in 1976. [1] It is a quick and accurate [ 2 ] spectroscopic analytical procedure used to measure the concentration of protein in a solution.

  4. 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]).

  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. Green fluorescent protein - Wikipedia

    en.wikipedia.org/wiki/Green_fluorescent_protein

    smURFP has a large extinction coefficient (180,000 M −1 cm −1) and has a modest quantum yield (0.20), which makes it comparable biophysical brightness to eGFP and ~2-fold brighter than most red or far-red fluorescent proteins derived from coral.

  7. Aromatic amino acid - Wikipedia

    en.wikipedia.org/wiki/Aromatic_amino_acid

    [1] [2] Most proteins absorb at 280 nm due to the presence of tyrosine and tryptophan. Of the aromatic amino acids, tryptophan has the highest extinction coefficient; its absorption maximum occurs at 280 nm. The absorption maximum of tyrosine occurs at 274 nm. [3]

  8. Fluorescence in the life sciences - Wikipedia

    en.wikipedia.org/wiki/Fluorescence_in_the_life...

    The quantum yield is an indicator of the efficiency of the dye (it is the ratio of emitted photons per absorbed photon), and the extinction coefficient is the amount of light that can be absorbed by a fluorophore. Both the quantum yield and extinction coefficient are specific for each fluorophore and multiplied together calculates the ...

  9. Extinction coefficient - Wikipedia

    en.wikipedia.org/wiki/Extinction_coefficient

    Extinction coefficient refers to several different measures of the absorption of light in a medium: Attenuation coefficient , sometimes called "extinction coefficient" in meteorology or climatology Mass extinction coefficient , how strongly a substance absorbs light at a given wavelength, per mass density