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Biuret test. In chemistry, the biuret test (IPA: / ˌbaɪjəˈrɛt /, / ˈbaɪjəˌrɛt / [1]), also known as Piotrowski's test, is a chemical test used for detecting the presence of at least two peptide bonds in a molecule. In the presence of peptides, a copper (II) ion forms mauve -colored coordination complexes in an alkaline solution.
The method combines the reactions of copper ions with the peptide bonds under alkaline conditions (the Biuret test) with the oxidation of aromatic protein residues. The Lowry method is based on the reaction of Cu +, produced by the oxidation of peptide bonds, with Folin–Ciocalteu reagent (a mixture of phosphotungstic acid and phosphomolybdic acid in the Folin–Ciocalteu reaction).
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.
While it is possible to analyze these proteins individually, total protein is a relatively quick and inexpensive analysis that does not discriminate by protein type. The traditional method for measuring total protein uses the biuret reagent , but other chemical methods such as dye-binding and refractometry are now available.
Biuret (/ ˈbjurɛt / BYUR-ret) is a chemical compound with the chemical formula HN (CONH2)2. It is a white solid that is soluble in hot water. A variety of organic derivatives are known. The term "biuret" also describes a family of organic compounds with the chemical formula R1R2N−C (=O)−N (R3)−C (=O)−NR4R5, where R1, R2, R3, R4 and R5 ...
Protein methods are the techniques used to study proteins. There are experimental methods for studying proteins (e.g., for detecting proteins, for isolating and purifying proteins, and for characterizing the structure and function of proteins, often requiring that the protein first be purified). Computational methods typically use computer ...
Proteins that have high hydrophobic amino acid content on the surface have low solubility in an aqueous solvent. Charged and polar surface residues interact with ionic groups in the solvent and increase the solubility of a protein. Knowledge of a protein's amino acid composition will aid in determining an ideal precipitation solvent and methods.
Quantitative proteomics is an analytical chemistry technique for determining the amount of proteins in a sample. [1][2][3][4] The methods for protein identification are identical to those used in general (i.e. qualitative) proteomics, but include quantification as an additional dimension. Rather than just providing lists of proteins identified ...