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Updated: Aug 14, 2026

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Published on: November 16, 2015
Characterization of monomeric and dimeric B domain of Staphylococcal protein A
A Karimi1, M Matsumura, P E Wright
1Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
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.
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