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Effects of Serine-to-Cysteine Mutations on β-Lactamase Folding
B. licheniformis exo-small β-lactamase (ESBL) has two nonsequential domains and a complex architecture. We replaced ESBL serine residues 126 and 265 with cysteine to probe the conformation of buried regions in each domain. Spectroscopic, hydrodynamic, and chemical methods revealed that the mutations...
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| Main Authors: | , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
The Biophysical Society
2007
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1948053/ https://ncbi.nlm.nih.gov/pubmed/17496026 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.106.103804 |
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