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There are three amino acids with side chains that are cations at neutral pH: arginine (Arg, R), lysine (Lys, K) and histidine (His, H). Arginine has a charged guanidino group and lysine a charged alkyl amino group, and are fully protonated at pH 7.
Pleckstrin homology domain(PH domain) or (PHIP) is a protein domainof approximately 120 amino acidsthat occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton. [1][2][3][4][5][6][7] This domain can bind phosphatidylinositollipids within biological membranes (such as phosphatidylinositol (3 ...
Like other amino acids, tryptophan is a zwitterion at physiological pH where the amino group is protonated (– NH + 3; pK a = 9.39) and the carboxylic acid is deprotonated ( –COO −; pK a = 2.38). [5] Humans and many animals cannot synthesize tryptophan: they need to obtain it through their diet, making it an essential amino acid.
Hydrophobicity scales. Hydrophobicity scales are values that define the relative hydrophobicity or hydrophilicity of amino acid residues. The more positive the value, the more hydrophobic are the amino acids located in that region of the protein. These scales are commonly used to predict the transmembrane alpha-helices of membrane proteins.
Lysine (symbol Lys or K) [2] is an α-amino acid that is a precursor to many proteins.It contains an α-amino group (which is in the protonated −NH + 3 form when dissolved in water), an α-carboxylic acid group (which is in the deprotonated −COO − form when dissolved in water), and a side chain lysyl ((CH 2) 4 NH 2), classifying it as a basic, charged (at physiological pH), aliphatic ...
The pH-dependence of the activity displayed by enzymes and the pH-dependence of protein stability, for example, are properties that are determined by the pK a values of amino acid side chains. The p K a values of an amino acid side chain in solution is typically inferred from the p K a values of model compounds (compounds that are similar to ...
Arginine is the amino acid with the formula (H 2 N)(HN)CN(H)(CH 2) 3 CH(NH 2)CO 2 H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO 2 −) and both the amino and guanidino groups are protonated, resulting in a cation.
Isoelectric point. The isoelectric point ( pI, pH (I), IEP ), is the pH at which a molecule carries no net electrical charge or is electrically neutral in the statistical mean. The standard nomenclature to represent the isoelectric point is pH (I). [ 1] However, pI is also used. [ 2] For brevity, this article uses pI.
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