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...
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| Gepubliceerd in: | Infect Immun |
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| Hoofdauteurs: | , , , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
American Society for Microbiology (ASM)
1994
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| Onderwerpen: | |
| Online toegang: | 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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