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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.
RGG motifs are primarily involved in mediating protein-RNA interactions.Positive charges from arginine residues promote electrostatic interactions with mRNA molecules. The composition and structure of the arginine side chain may also allow for specific interactions with other molecules as opposed to the other positively charged amino acids, lysine and histidine. [4]
Other names Iminomethanediamine. ... including on the side chain of arginine. Structure. Guanidine can be thought of as a nitrogenous analogue of carbonic acid.
Next, the arginine side chain of the target protein then acts a nucleophile, attacking the electrophilic carbon adjacent to the oxonium ion. In order for this step to occur, the arginine nucleophile is deprotonated by a glutamate residue on the catalyzing enzyme [disputed – discuss]. Another conserved glutamate residue forms a hydrogen bond ...
In arginylation, arginine (pictured above) is added to proteins. Arginylation is a post-translational modification in which proteins are modified by the addition of arginine (Arg) at the N-terminal amino group or side chains of reactive amino acids by the enzyme, arginyltransferase (ATE1). Recent studies have also revealed that hundreds of ...
Lys is essential for humans, and behaves similarly to arginine. It contains a long, flexible side chain with a positively charged end. The flexibility of the chain makes lysine and arginine suitable for binding to molecules with many negative charges on their surfaces. E.g., DNA-binding proteins have their active regions rich with arginine and ...
In the reaction from arginine to citrulline, one of the terminal nitrogen atoms of the arginine side chain is replaced by an oxygen. Thus, arginine's positive charge (at physiological pH) is removed, altering the protein's tertiary structure. The reaction uses one water molecule and yields ammonia as a side-product:
N-linked glycans attached to a nitrogen of asparagine or arginine side-chains. N-linked glycosylation requires participation of a special lipid called dolichol phosphate. O-linked glycans attached to the hydroxyl oxygen of serine, threonine, tyrosine, hydroxylysine, or hydroxyproline side-chains, or to oxygens on lipids such as ceramide.