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Valine (symbol Val or V) [4] is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH 3 + form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side chain isopropyl group, making it a non-polar aliphatic amino acid.
Chemical properties: XLogP: -2.193: pI: 5.96: ... ^a EINECS for Valine ^a CID 71563 from PubChem ^a CID 1182 from PubChem This page was last edited on 11 ...
The unity of the chemical category was recognized by Wurtz in 1865, but he gave no particular name to it. [17] The first use of the term "amino acid" in the English language dates from 1898, [18] while the German term, Aminosäure, was used earlier. [19] Proteins were found to yield amino acids after enzymatic digestion or acid hydrolysis.
Following is a table listing the one-letter symbols, the three-letter symbols, and the chemical properties of the side chains of the standard amino acids. The masses listed are based on weighted averages of the elemental isotopes at their natural abundances. Forming a peptide bond results in elimination of a molecule of water. Therefore, the ...
A branched-chain amino acid (BCAA) is an amino acid having an aliphatic side-chain with a branch (a central carbon atom bound to three or more carbon atoms). Among the proteinogenic amino acids, there are three BCAAs: leucine, isoleucine, and valine. [1] Non-proteinogenic BCAAs include 2-aminoisobutyric acid and alloisoleucine.
Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. [1] The two most common secondary structural elements are alpha helices and beta sheets, though beta turns and omega loops occur as well. Secondary structure elements typically spontaneously form as an intermediate before the ...
Alpha helix. Three-dimensional structure of an alpha helix in the protein crambin. An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the secondary structure of proteins. It is also the most extreme type of local structure ...
Norvaline (abbreviated as Nva) is an amino acid with the formula CH 3 (CH 2) 2 CH (NH 2)CO 2 H. The compound is a structural analog of valeric acid and also an isomer of the more common amino acid valine. [2] Like most other α-amino acids, norvaline is chiral. It is a white, water-soluble solid.
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