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Cold Instability of Aponeocarzinostatin and its Stabilization by Labile Chromophore
The conformational stability of aponeocarzinostatin, an all-β-sheet protein with 113 amino-acid residues, is investigated by thermal-induced equilibrium unfolding between pH 2.0 and 10.0 with and without urea. At room temperature, the protein is stable in a pH range of 4.0–10.0, whereas the stabilit...
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| Главные авторы: | , , , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
Biophysical Society
2005
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1305655/ https://ncbi.nlm.nih.gov/pubmed/15821162 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.104.051722 |
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