Results 1–4 of 4 for nukleofil
Nucleophiles are negatively charged or bear a partial negative charge. Examples are lone pairs or a hydroxide ion.
Cysteine is neutral amino acids with polar side chains. Because of its high reactivity, the thiol group of cysteine has numerous biological functions. It serves as a potent nucleophile and metal ligand (particularly for iron and zinc), but is best known for its ability to form disulfide bonds, which often make an important contribution to the stability of extracellular proteins. Cysteine is a non-essential amino acid, which means that it is biosynthesized in humans.
Serine is neutral amino acids with polar side chains. It is one of two hydroxyl amino acids. Both are commonly considered to by hydrophilic due to the hydrogen bonding capacity of the hydroxyl group. Serine often serves as a nucleophile in many enzyme active sites, and is best known for its role in the serine proteases. Serine is a site of phosphorylation and glycosylation which is important for enzyme regulation and cell signaling. It is not essential to the human diet, since it is synthesized in the body from other metabolites, including glycine.
Tyrosine is hydrophobic amino acids with aromatic side chain. Tyrosine is large aromatic residue that is normally found buried in the interior of a protein and is important for protein stability. Tyrosine has special properties since its hydroxyl side chain may function as a powerful nucleophile in an enzyme active site (when ionized) and is a common site for phosphorylation in cell signaling cascades. Tyrosine absorbs ultraviolet radiation and contributes to the absorbance spectra of proteins. It is not essential (or semi-essential) to the human diet, since it is synthesized in the body from other metabolites.
Generalic, Eni. "Nukleofil." Croatian-English Chemistry Dictionary & Glossary. 29 June 2022. KTF-Split. {Date of access}. <https://glossary.periodni.com>.
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Periodic Table