Two disulfide mutants in domain I of Bacillus thuringiensis Cry3Aa δ-endotoxin increase stability with no effect on toxicity
To increase protein stability and test protein function, three double-cysteine mutations were individually introduced by protein engineering into the cysteinefree Cry3Aa δ-endotoxin from Bacillus thuringiensis. These mutations were designed to create disulfide bonds between α-helices 2 and 5 (posit...
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| Institution: | Universidad EIA |
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| Main Authors: | , , , , |
| Format: | Artículo de revista |
| Language: | English |
| Published: |
2012-05
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| Subjects: | |
| Online Access: | https://repositorio.udes.edu.co/handle/001/3659 |
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