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  2. Molar absorption coefficient - Wikipedia

    en.wikipedia.org/wiki/Molar_absorption_coefficient

    In chemistry, the molar absorption coefficient or molar attenuation coefficient ( ε) [ 1] is a measurement of how strongly a chemical species absorbs, and thereby attenuates, light at a given wavelength. It is an intrinsic property of the species. The SI unit of molar absorption coefficient is the square metre per mole ( m2/mol ), but in ...

  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. The reaction is dependent on the amino acid composition of the measured proteins.

  4. Bovine serum albumin - Wikipedia

    en.wikipedia.org/wiki/Bovine_serum_albumin

    Bovine serum albumin (BSA or "Fraction V") is a serum albumin protein derived from cows. It is often used as a protein concentration standard in lab experiments. The nickname "Fraction V" refers to albumin being the fifth fraction of the original Edwin Cohn purification methodology that made use of differential solubility characteristics of plasma proteins.

  5. 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. Molar extinction coefficient, how ...

  6. 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]

  7. Flavin adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_dinucleotide

    In biochemistry, flavin adenine dinucleotide ( FAD) is a redox -active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may be in the form of FAD or flavin mononucleotide (FMN). Many flavoproteins are known: components of ...

  8. Green fluorescent protein - Wikipedia

    en.wikipedia.org/wiki/Green_fluorescent_protein

    The green fluorescent protein ( GFP) is a protein that exhibits green fluorescence when exposed to light in the blue to ultraviolet range. [ 2][ 3] The label GFP traditionally refers to the protein first isolated from the jellyfish Aequorea victoria and is sometimes called avGFP. However, GFPs have been found in other organisms including corals ...

  9. Phycocyanin - Wikipedia

    en.wikipedia.org/wiki/Phycocyanin

    Phycocyanin. Phycocyanin is a pigment -protein complex from the light-harvesting phycobiliprotein family, along with allophycocyanin and phycoerythrin. [ 1] It is an accessory pigment to chlorophyll. All phycobiliproteins are water-soluble, so they cannot exist within the membrane like carotenoids can. Instead, phycobiliproteins aggregate to ...