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Identification of Folding Intermediates of Streblin, The Most Stable Serine Protease: Biophysical Analysis
Streblin, a serine proteinase from plant Streblus asper, has been used to investigate the conformational changes induced by pH, temperature, and chaotropes. The near/far UV circular dichroism activities under fluorescence emission spectroscopy and 8-aniline-1-naphthalene sulfonate (ANS) binding have...
Tallennettuna:
| Päätekijät: | , , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Springer US
2013
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3918384/ https://ncbi.nlm.nih.gov/pubmed/24108566 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s12010-013-0565-8 |
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