title: Characterization of monomeric and dimeric B domain of Staphylococcal protein A.
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.
authors.affiliation: Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
authors.forename: A
authors.initials: A
authors.lastname: Karimi
authors.forename: M
authors.initials: M
authors.lastname: Matsumura
authors.forename: P E
authors.initials: PE
authors.lastname: Wright
authors.forename: H J
authors.initials: HJ
authors.lastname: Dyson
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D019281:Dimerization; D005454:Fluorescence Polarization; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D013205:Staphylococcal Protein A / Q000737:chemistry*
chemical_list: D011994:Recombinant Proteins; D013205:Staphylococcal Protein A