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BPTI folding revisited: switching a disulfide into methylene thioacetal reveals a previously hidden path
Bovine pancreatic trypsin inhibitor (BPTI) is a 58-residue protein that is stabilized by three disulfide bonds at positions 5–55, 14–38 and 30–51. Widely studied for about 50 years, BPTI represents a folding model for many disulfide-rich proteins. In the study described below, we replaced the solven...
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| 出版年: | Chem Sci |
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| 主要な著者: | , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Royal Society of Chemistry
2018
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5982216/ https://ncbi.nlm.nih.gov/pubmed/29910933 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1039/c8sc01110a |
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