Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding.
The DNA binding properties of 52 different single-amino acid substitutions in lambda repressor's amino-terminal domain have been characterized. Seven proteins bearing mutations that change solvent-exposed side chains have been purified. The amino-terminal domains of these mutant repressors are folde...
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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1983
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC393890/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6221342/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.80.9.2676 |
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