pCys47Asp

pCys47Asp is a designation used in protein science to indicate a point mutation at residue 47, in which a cysteine is replaced by an aspartic acid. In some sources this substitution is written C47D and may be referred to as a pCys47Asp mutation to emphasize the protein context. Because nomenclature varies by database and publication, readers should consult the accompanying annotation to confirm the exact meaning.

In experimental mutagenesis, pCys47Asp is used to probe the role of the cysteine at position 47. Cysteine can participate in disulfide bonding, metal coordination, or redox chemistry, and replacing it with aspartic acid introduces a negative charge and a different side-chain geometry, which can affect folding, stability, catalysis, or ligand binding.

Detection and validation typically involve DNA sequencing to confirm the substitution, and proteomic approaches such as mass spectrometry to verify the amino-acid change at position 47. Structural analyses, including X-ray crystallography or cryo-EM, and functional assays, help assess the impact on the protein’s activity and interactions.

As with other mutation designations, the precise interpretation of pCys47Asp depends on the protein in question and the source. Cross-check with the original report to determine the effect on function and structure. See also C47D, site-directed mutagenesis, and protein engineering.