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Functional Unfolding of α(1)-Antitrypsin Probed by Hydrogen-Deuterium Exchange Coupled with Mass Spectrometry
The native state of α(1)-antitrypsin (α(1)AT), a member of the serine protease inhibitor (serpin) family, is considered a kinetically trapped folding intermediate that converts to a more stable form upon complex formation with a target protease. Although previous structural and mutational studies of...
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| Main Authors: | , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
American Society for Biochemistry and Molecular Biology
2009
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2689767/ https://ncbi.nlm.nih.gov/pubmed/19136720 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/mcp.M800365-MCP200 |
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