Histidine residues near the N terminus of staphylococcal alpha-toxin as reporters of regions that are critical for oligomerization and pore formation.
Chemical modification of histidine residues in staphylococcal alpha-toxin leads to loss of functional activity. Site-directed mutants of the toxin in which each of the four histidine residues was replaced by several amino acids were therefore produced. The mutant proteins were purified and character...
Guardado en:
| Publicado en: | Infect Immun |
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| Autores principales: | , , , , , , |
| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
American Society for Microbiology (ASM)
1994
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC186505/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8188346/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/iai.62.6.2249-2256.1994 |
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