dc.contributor.author | Vandergoot, F.G. | fr_FR |
dc.contributor.author | Pattus, F. | fr_FR |
dc.date.accessioned | 2013-02-18T16:17:33Z | |
dc.date.available | 2013-02-18T16:17:33Z | |
dc.date.issued | 1993 | fr_FR |
dc.identifier.citation | Vandergoot, F.G. ; Pattus, F., Modèle d'étude de l'insertion des protéines membranaires, Med Sci (Paris), 1993, Vol. 9, N° 2; p.171-178 | fr_FR |
dc.identifier.issn | 1958-5381 | fr_FR |
dc.identifier.uri | http://hdl.handle.net/10608/2890 | |
dc.description.abstract | Colicin A from Citrobacter freundii and aerolysin from Aeromonas hydrophila are representative of two classes of pore-forming toxins. Colicin A, an alpha-helical protein, contains an hydrophobic hairpin which is buried inside the structure in solution. It is an << inside out >> membrane protein. Aerolysin is formed almost exclusively of beta-sheet and possesses a very hydrophilic amino acid sequence. It is secreted as an inactive precursor which is activated by proteolytic removal of about 41-43 residues from the C-terminus. The mechanism of membrane insertion and the structure of the membrane bound form of these toxins are discussed. | fr |
dc.language.iso | fr | fr_FR |
dc.publisher | John Libbey Eurotext, Montrouge | fr_FR |
dc.rights | Article en libre accès | fr |
dc.rights | Médecine/Sciences - Inserm - SRMS | fr |
dc.source | M/S. Médecine sciences [revue papier, ISSN : 0767-0974], 1993, Vol. 9, N° 2; p.171-178 | fr_FR |
dc.title | Modèle d'étude de l'insertion des protéines membranaires | fr |
dc.type | Article | fr_FR |
dc.identifier.doi | 10.4267/10608/2890 | |