Article révisé par les pairs
Titre:
  • The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces.
Auteur:Van Molle, Inge; Moonens, Kristof; Buts, Lieven; Garcia-Pino, Abel; Panjikar, Santosh; Wyns, Lode; De Greve, Henri; Bouckaert, Julie
Informations sur la publication:Acta crystallographica. Section D, Biological crystallography, 65, Pt 5, page (411-420)
Statut de publication:Publié, 2009-05
Sujet CREF:Sciences bio-médicales et agricoles
MeSH keywords:Adhesins, Escherichia coli -- chemistry
Calorimetry, Differential Scanning
Cross-Linking Reagents -- pharmacology
Crystallography, X-Ray
Dimerization
Escherichia coli -- chemistry -- genetics
Escherichia coli Proteins -- chemistry -- genetics -- isolation & purification -- metabolism
Fimbriae Proteins -- metabolism
Glutaral -- pharmacology
Models, Molecular
Molecular Chaperones -- chemistry -- genetics -- isolation & purification -- metabolism
Nephelometry and Turbidimetry
Protein Conformation
Protein Denaturation
Protein Interaction Mapping
Recombinant Fusion Proteins -- chemistry -- isolation & purification
Note générale:FLWNA
Langue:Anglais
Identificateurs:urn:issn:0907-4449
info:doi/10.1107/S0907444909005174
info:pii/S0907444909005174
info:pmid/19390146