Structurally conserved aromaticity of Tyr249 and Phe 264 in helix 7 is important for toxicity of the Bacillus thuringiensis Cry4Ba toxin
Functional elements of the conserved helix 7 in the poreforming domain of the Bacillus thuringiensis Cry δ-endotoxins have not yet been clearly identified. Here, we initially performed alanine substitutions of four highly conserved aromatic residues, Trp243, Phe246, Tyr 249 and Phe264, in helix 7 of...
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Main Authors: | , |
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Format: | Article |
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2018
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Online Access: | https://repository.li.mahidol.ac.th/handle/123456789/24234 |
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Institution: | Mahidol University |
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