Y184F

Y184F indicates a missense mutation in which the amino acid tyrosine (Y) at position 184 is replaced by phenylalanine (F) in a protein sequence. The notation is used in genetics, biochemistry, and structural biology to describe single-residue substitutions.

This change is chemically conservative: tyrosine and phenylalanine both have bulky aromatic rings, but tyrosine bears a phenolic hydroxyl group. Removal of the hydroxyl can affect phosphorylation potential, hydrogen bonding, and potentially interactions with substrates, cofactors, or other protein regions.

The functional impact is context-dependent. If residue 184 lies near an active site, substrate-binding pocket, or protein–protein interface, Y184F can alter catalytic efficiency, binding affinities, or stability. In mutational studies, researchers report changes in kinetic parameters, folding stability, or interaction strength.

In literature, Y184F has been observed in various proteins; its significance is determined by structural data (X-ray, cryo-EM), sequence conservation, and functional assays. For precise interpretation, consult protein-specific databases (UniProt, PDB) and primary studies describing the mutation in the relevant protein context.