Pore Formation by Nisin Involves Translocation of Its C-Terminal Part across the Membrane

Nisin is an amphiphilic peptide with a strong antimicrobial activity against various Gram-positive bacteria. Its activity results from permeabilization of bacterial membranes, causing efflux of cytoplasmic compounds. To get information on the molecular mechanism of membrane permeabilization, a mutan...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Biochemistry (Easton) 1998-11, Vol.37 (46), p.16033-16040
Hauptverfasser:	van Kraaij, Cindy, Breukink, Eefjan, Noordermeer, Minke A, Demel, Rudy A, Siezen, Roland J, Kuipers, Oscar P, de Kruijff, Ben
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Anions Anti-Bacterial Agents - metabolism Anti-Bacterial Agents - pharmacology Biological Transport - genetics Cell Membrane - genetics Cell Membrane - metabolism Cell Membrane Permeability - genetics Histidine - genetics Hydrogen-Ion Concentration Membrane Lipids - metabolism Molecular Sequence Data Mutagenesis, Site-Directed nisin Nisin - analogs & derivatives Nisin - genetics Nisin - metabolism Nisin - pharmacology Peptide Fragments - genetics Peptide Fragments - metabolism Peptide Fragments - pharmacology Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!