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Temperature-dependent conformational change affecting Tyr11 and sweetness loops of brazzein
The sweet protein brazzein, a member of the Csβα fold family, contains four disulfide bonds that lend a high degree of thermal and pH stability to its structure. Nevertheless, a variable temperature study has revealed that the protein undergoes a local, reversible conformational change between 37 an...
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| 主要な著者: | , , , , , , , |
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| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
2013
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3982881/ https://ncbi.nlm.nih.gov/pubmed/23349025 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/prot.24259 |
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