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Histidine (symbol His or H) [2] is an essential 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), a carboxylic acid group (which is in the deprotonated –COO − form under biological conditions), and an imidazole side chain (which is partially protonated), classifying it as a ...
Aromatic amino acids often serve as the precursors to important biochemicals. Histidine is the precursor to histamine.; Tryptophan is the precursor to 5-hydroxytryptophan and then serotonin, tryptamine, auxin, kynurenines, and melatonin.
Nonpolar Neutral 1.8 89.094 8.76 GCN Arginine: Arg R Fixed cation Basic polar Positive −4.5 174.203 5.78 MGR, CGY [54] Asparagine: Asn N Amide Polar Neutral −3.5 132.119 3.93 AAY Aspartate: Asp D Anion Brønsted base: Negative −3.5 133.104 5.49 GAY Cysteine: Cys C Thiol Brønsted acid Neutral 2.5 250 0.3 121.154 1.38 UGY Glutamine: Gln Q ...
The endothelial protease vasohibin [f] uses a cysteine as the nucleophile, but a serine to coordinate the histidine base. [43] [44] Despite the serine being a poor acid, it is still effective in orienting the histidine in the catalytic triad. [43] Some homologues alternatively have a threonine instead of serine at the acid location. [43]
Vapor phases represent the simplest non polar phases, because it has no interaction with the solute. [18] The hydration potential and its correlation to the appearance of amino acids on the surface of proteins was studied by Wolfenden. Aqueous and polymer phases were used in the development of a novel partitioning scale. [19]
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.
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).
When comparing a polar and nonpolar molecule with similar molar masses, the polar molecule in general has a higher boiling point, because the dipole–dipole interaction between polar molecules results in stronger intermolecular attractions. One common form of polar interaction is the hydrogen bond, which is also