Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Characterization of monomeric and dimeric B domain of Staphylococcal protein A

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Karimi, A.
  • Matsumura, M.
  • Wright, Peter
  • Dyson, Jane

publication date

  • October 1999

journal

  • Journal of Peptide Research  Journal

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.

subject areas

  • Amino Acid Sequence
  • Circular Dichroism
  • Dimerization
  • Fluorescence Polarization
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Folding
  • Recombinant Proteins
  • Sequence Homology, Amino Acid
  • Staphylococcal Protein A
scroll to property group menus

Research

keywords

  • CD
  • NMR
  • bound water
  • fluorescence
  • three-helix bundle topology
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 1397-002X

Digital Object Identifier (DOI)

  • 10.1034/j.1399-3011.1999.00115.x

PubMed ID

  • 10532240
scroll to property group menus

Additional Document Info

start page

  • 344

end page

  • 352

volume

  • 54

issue

  • 4

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support