Asp96

Asp96 is a designation used in protein science to refer to the aspartic acid residue at position 96 in a given protein sequence. In standard residue numbering, each amino acid is assigned a position, and the residue at position 96 is abbreviated as D96 or Asp96 in literature and databases. The exact identity and context of Asp96 depend on the specific protein and its sequence, including any isoforms or post-translational processing that may affect numbering.

The functional role of Asp96 varies with the protein. Aspartic acid residues are acidic and often participate in catalytic activity, substrate binding, metal coordination, or the stabilization of structural motifs through hydrogen bonding and salt-bridge networks. The placement of Asp96 within the three-dimensional structure determines whether it acts in catalysis, participates in a binding pocket, or contributes to the overall stability of the protein.

In research, Asp96 is often investigated through mutational analysis (for example, substituting Asp96 with alanine) to assess its importance for activity, binding, or stability. Structural biologists examine the environment around Asp96 in three-dimensional models to understand interactions with cofactors, substrates, or neighboring residues. Conservation of Asp96 across homologous proteins can indicate functional significance, whereas variability may suggest a more peripheral role.

Databases such as UniProt and the Protein Data Bank (PDB) record Asp96 according to the sequence used in a given entry. It is important to verify the exact numbering in a study, as different isoforms, signal peptides, or processing steps can shift residue positions. Overall, Asp96 serves as a reference point for describing the role of a specific aspartic acid residue within a protein.