Surface histidine and aspartate residues on model proteins

Surface histidine and aspartate residues on model proteins refer to specific amino acid side chains located on the solvent-accessible exterior of proteins used in experimental research, such as bovine serum albumin, lysozyme, or myoglobin (PubMed: 1886587). These residues are primarily studied for their ability to coordinate with transition metal ions (e.g., Cu2+, Ni2+, Zn2+), a property that forms the basis of immobilized metal affinity chromatography (IMAC) and metal-affinity aqueous two-phase partitioning (PubMed: 1659777). Histidine's imidazole ring and aspartate's carboxylate group serve as electron donors to form coordination bonds with metals, which is a critical feature in protein purification and structural characterization. In a biological context, these surface residues contribute to the protein's solubility, charge distribution, and interaction with the surrounding environment. However, this term does not describe a specific therapeutic target or a unique biological receptor; rather, it describes a general structural feature used in biophysical and biochemical studies to model protein behavior. Consequently, there are no therapeutic drugs that specifically target these residues for the treatment of disease (PubMed: 1557030).

Other names

Surface-exposed histidine and aspartate residuesExposed amino acid side chainsMetal-binding surface residues