Expression, purification, and functional characterization of the carboxyl-terminal domain fragment of bacteriophage 434 repressor.
The repressor protein of bacteriophage 434 binds to DNA as a dimer of identical subunits. Its strong dimerization is mediated by the carboxyl-terminal domain. Cooperative interactions between the C-terminal domains of two repressor dimers bound at adjacent sites can stabilize protein-DNA complexes f...
محفوظ في:
| الحاوية / القاعدة: | J Bacteriol |
|---|---|
| المؤلفون الرئيسيون: | , |
| التنسيق: | Artigo |
| اللغة: | Inglês |
| منشور في: |
American Society for Microbiology (ASM)
1994
|
| الموضوعات: | |
| الوصول للمادة أونلاين: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC197060/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7961451/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.176.22.6907-6914.1994 |
| الوسوم: |
لا توجد وسوم, كن أول من يضع وسما على هذه التسجيلة!
|