molecular pin to study the dynamics of β-barrel formation in pore-forming toxins on erythrocytes: a sliding model

γ-Hemolysins are pore-forming toxins which develop from water-soluble monomers by combining two different 'albeit homologous' proteins. They form oligomeric pores in both cell and model membranes by undergoing a still poorly understood conformational rearrangement in the stem region. The s...

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Veröffentlicht in:	Cellular and molecular life sciences : CMLS 2008-01, Vol.65 (2), p.312-323
Hauptverfasser:	Viero, G, Gropuzzo, A, Joubert, O, Keller, D, Prévost, G, Dalla Serra, M
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Biochemistry Biomedical and Life Sciences Biomedicine Cell Biology Cysteine Cysteine - genetics Disulfides Disulfides - metabolism Electrophysiology Erythrocyte Membrane Erythrocyte Membrane - metabolism Erythrocytes Erythrocytes - metabolism hemolysin Hemolysin Proteins Hemolysin Proteins - chemistry Hemolysin Proteins - metabolism Hemolysis Humans Kinetics Life Sciences membrane protein Membranes, Artificial Models, Biological Mutant Proteins Mutant Proteins - metabolism Mutation Mutation - genetics Oxidation-Reduction Pore-forming toxin protein motion Protein Structure, Secondary Rabbits Research Article Temperature Time Factors β-barrel
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