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In organic chemistry and biochemistry, a side chain is a chemical group that is attached to a core part of the molecule called the "main chain" or backbone. The side chain is a hydrocarbon branching element of a molecule that is attached to a larger hydrocarbon backbone. It is one factor in determining a molecule's properties and reactivity. [2 ...
This occurs halfway between the two carboxylate pK a values: pI = 1 / 2 (pK a1 + pK a(R)), where pK a(R) is the side chain pK a. [38] Similar considerations apply to other amino acids with ionizable side-chains, including not only glutamate (similar to aspartate), but also cysteine, histidine, lysine, tyrosine and arginine with positive ...
Side-chain, side chain, or sidechain may refer to: Side chain, a chemical group attached to the main chain or backbone of a molecule, such as a protein; Substituent, an atom or group of atoms substituted in place of a hydrogen atom on the parent chain of a hydrocarbon; Side-chaining, an effect in digital audio processing
The ability of the Coomassie dye to target amino acids with aromatic groups (phenylalanine, tyrosine, tryptophan) and basic side chains (lysine, arginine and histidine) allows the Bradford assay to be used for fingerprint analysis. The assay was successfully used to identify the biological sex of the fingerprint. Female samples were shown to ...
Only proline differs from this basic structure as its side chain is cyclical, bonding to the amino group, limiting protein chain flexibility. [34] The side chains of the standard amino acids have a variety of chemical structures and properties, and it is the combined effect of all amino acids that determines its three-dimensional structure and ...
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 ...
Side chain Hydro-phobic pKa § Polar pH Small Tiny Aromatic or Aliphatic van der Waals volume (Å 3) Alanine: A Ala -CH 3 - - Aliphatic 67 Cysteine: C Cys -CH 2 SH: 8.55 acidic - 86 Aspartic acid: D Asp -CH 2 COOH 3.67 acidic - 91 Glutamic acid: E Glu -CH 2 CH 2 COOH 4.25 acidic - 109 Phenylalanine: F Phe -CH 2 C 6 H 5 - - Aromatic 135 Glycine ...
The folding is driven by the non-specific hydrophobic interactions, the burial of hydrophobic residues from water, but the structure is stable only when the parts of a protein domain are locked into place by specific tertiary interactions, such as salt bridges, hydrogen bonds, and the tight packing of side chains and disulfide bonds.