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α-Lytic protease can exist in two separately stable conformations with different His(57) mobilities and catalytic activities
α-Lytic protease is a bacterial serine protease widely studied as a model system of enzyme catalysis. Here we report that lyophilization induces a structural change in the enzyme that is not reversed by redissolution in water. The structural change reduces the mobility of the active-site histidine r...
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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: |
National Academy of Sciences
2005
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC545854/ https://ncbi.nlm.nih.gov/pubmed/15657134 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0409279102 |
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