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  2. Hopkins–Cole reaction - Wikipedia

    en.wikipedia.org/wiki/HopkinsCole_reaction

    The Hopkins-Cole reaction, also known as the glyoxylic acid reaction, is a chemical test used for detecting the presence of tryptophan in proteins. [1] A protein solution is mixed with Hopkins Cole reagent, which consists of glyoxylic acid. Concentrated sulfuric acid is slowly added to form two layers. A purple ring appears between the two ...

  3. Sakaguchi test - Wikipedia

    en.wikipedia.org/wiki/Sakaguchi_test

    Sakaguchi test. The Sakaguchi test is a chemical test used to detect presence of arginine in proteins. It is named after the Japanese food scientist and organic chemist, Shoyo Sakaguchi (1900–1995) who described the test in 1925. [1] The Sakaguchi reagent used in the test consists of 1-Naphthol and a drop of sodium hypobromite.

  4. Adamkiewicz reaction - Wikipedia

    en.wikipedia.org/wiki/Adamkiewicz_reaction

    Adamkiewicz reaction. The Adamkiewicz reaction is part of a biochemical test used to detect the presence of the amino acid tryptophan in proteins. When concentrated sulfuric acid is combined with a solution of protein and glyoxylic acid, a red/purple colour is produced. It was named after its discoverer, Albert Wojciech Adamkiewicz.

  5. Peptide synthesis - Wikipedia

    en.wikipedia.org/wiki/Peptide_synthesis

    In organic chemistry, peptide synthesis is the production of peptide molecules by chemical means. Formally, alpha- amino acids are condensed with the exclusion of water molecules, to form linear chains in which the amino acids are linked by amide bonds. The amide bond between two alpha amino acids is known as a peptide bond.

  6. Edman degradation - Wikipedia

    en.wikipedia.org/wiki/Edman_degradation

    Edman degradation. Edman degradation, developed by Pehr Edman, is a method of sequencing amino acids in a peptide. [1] In this method, the amino-terminal residue is labeled and cleaved from the peptide without disrupting the peptide bonds between other amino acid residues.

  7. Protein phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphorylation

    Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or otherwise modifying its ...

  8. Erlenmeyer–Plöchl azlactone and amino-acid synthesis

    en.wikipedia.org/wiki/Erlenmeyer–Plöchl...

    The Erlenmeyer–Plöchl azlactone and amino acid synthesis, named after Friedrich Gustav Carl Emil Erlenmeyer who partly discovered the reaction, is a series of chemical reactions which transform an N - acyl glycine to various other amino acids via an oxazolone (also known as an azlactone). [1][2] Hippuric acid, the benzamide derivative of ...

  9. Xanthoproteic reaction - Wikipedia

    en.wikipedia.org/wiki/Xanthoproteic_reaction

    The xanthoproteic reaction is a method that can be used to detect a presence of protein soluble in a solution, using concentrated nitric acid. The test gives a positive result in amino acids carrying aromatic groups, especially in the presence of tyrosine. If the test is positive the proof is neutralized with an alkali, turning dark yellow.