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The structure of a disulfide bond can be described by its χ ss dihedral angle between the C β −S γ −S γ −C β atoms, which is usually close to ±90°. The disulfide bond stabilizes the folded form of a protein in several ways: It holds two portions of the protein together, biasing the protein towards the folded topology.
Since orthophosphoric acid has three −OH groups, it can esterify with one, two, or three alcohol molecules to form a mono-, di-, or triester. See the general structure image of an ortho- (or mono-) phosphate ester below on the left, where any of the R groups can be a hydrogen or an organic radical. Di- and tripoly- (or tri-) phosphate esters ...
6 These form water-stable salts. [12] The anion has an ethane-like structure and contains a P−P bond. The formal oxidation state of phosphorus is +4. The oxygen analogue is the hypodiphosphate anion, P 2 O 4− 6. P 3 S 3− 9 contains a six-membered P 3 S 3 ring. The ammonium salt is produced by reaction of P 4 S 10 in liquid ammonia. [13]
TCEP is often used as a reducing agent to break disulfide bonds within and between proteins as a preparatory step for gel electrophoresis.. Compared to the other two most common agents used for this purpose (dithiothreitol and β-mercaptoethanol), TCEP has the advantages of being odorless, a more powerful reducing agent, an irreversible reducing agent (in the sense that TCEP does not ...
The phosphate ion has a molar mass of 94.97 g/mol, and consists of a central phosphorus atom surrounded by four oxygen atoms in a tetrahedral arrangement. It is the conjugate base of the hydrogen phosphate ion H(PO 4) 2−, which in turn is the conjugate base of the dihydrogen phosphate ion H 2 (PO 4) −
Phosphoric acids produced from phosphate rock or thermal processes often requires purification. A common purification methods is liquid-liquid extraction, which involves the separation of phosphoric acids from water and other impurities using organic solvents, such as tributyl phosphate (TBP), methyl isobutyl ketone (MIBK), or n-octanol ...
Representation of an organic compound hydroxy group, where R represents a hydrocarbon or other organic moiety, the red and grey spheres represent oxygen and hydrogen atoms respectively, and the rod-like connections between these, covalent chemical bonds.
The thiol groups of the cysteine residues in proteins can be oxidized resulting in disulfide bridges with other cysteine side chains (and form cystine) and/or linkage of polypeptides. Disulfide bridges ( disulfide bonds ) make an important contribution to the structure of proteins.