Refined solution structure of the DNA-binding domain of GAL4 and use of3J(113Cd,1H) in structure determination
β Scribed by James D. Baleja; Venkataraman Thanabal; Gerhard Wagner
- Book ID
- 110369111
- Publisher
- Springer Netherlands
- Year
- 1997
- Tongue
- English
- Weight
- 154 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0925-2738
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The structure of the C-terminal DNA-binding domain of human immunovirus-1 integrase has been refined using nuclear magnetic resonance spectroscopy. The protein is a dimer in solution and shows a well-defined dimer interface. The folding topology of the monomer consists of a fivestranded β€-barrel tha
## Abstract FOXP1 belongs to the Pβsubfamily of forkhead transcription factors and contains a conserved forkhead DNAβbinding domain. According to size exclusion chromatography analysis, the forkhead domain of FOXP1 existed as a mixture of monomer and dimer. The dissociation constants of the forkhea