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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.
Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that joins the carboxyl group of one amino acid to the amine group of the next in a head-to-tail manner to form a polypeptide chain. The chain has two ends – an amine group, the N-terminus, and ...
2-, alpha-, or α-amino acids [21] have the generic formula H 2 NCHRCOOH in most cases, [b] where R is an organic substituent known as a "side chain". [22] Of the many hundreds of described amino acids, 22 are proteinogenic ("protein-building").
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.
Each amino acid has a carboxyl group and an amine group. Amino acids link to one another to form a chain by a dehydration reaction which joins the amine group of one amino acid to the carboxyl group of the next. Thus polypeptide chains have an end with an unbound carboxyl group, the C-terminus, and an end with an unbound amine group, the N ...
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A conservative replacement (also called a conservative mutation or a conservative substitution or a homologous replacement) is an amino acid replacement in a protein that changes a given amino acid to a different amino acid with similar biochemical properties (e.g. charge, hydrophobicity and size). [1] [2]
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