| MWexperimental | 39 | kDa |
| MWexpected | 23 | kDa |
| VPorod | 59 | nm3 |
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log I(s)
1.69×100
1.69×10-1
1.69×10-2
1.69×10-3
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s, nm-1
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An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFκB p50/RelA.
Baughman HER, Narang D, Chen W, Villagrán Suárez AC, Lee J, Bachochin MJ, Gunther TR, Wolynes PG, Komives EA, J Biol Chem :102349 (2022) Europe PMCSASDHD5 – Transactivation domain of RelA
Transcription factor p65 340-549|
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Fits and models
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Synchrotron SAXS data from solutions of the Nuclear factor kB RelA transactivation domain in 25 mM Tris.Cl, 150 mM NaCl, 1 mM DTT, 0.5 mM EDTA, pH 7.5 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.25 mg/ml was measured at 10°C. 32 successive 10 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. 32 successive 10 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
Storage temperature = UNKNOWN |
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