Characterization of monomeric and dimeric B domain of Staphylococcal protein A

Publisher Website
Google Scholar
Abstract
Both monomeric and dimeric constructs of the B domain of protein A from Staphylococcus aureus have been characterized by NMR, CD and fluorescence spectroscopy. The monomeric form of the protein was synthesized using a novel method incorporating the use of a recombinant, folded, chimeric protein. A comparison of the recombinant monomeric form with the commercially available dimeric form indicates that, although the dimer retains the integrity of the three‐helix bundle structure present in the monomer, there are interdomain contacts in the dimeric form. A single long‐lived water molecule in the hydrophobic core of the three‐helix bundle of monomeric protein A may represent an important stabilizing factor for the three‐helix bundle topology.