| MWexperimental | 98 | kDa |
| MWexpected | 94 | kDa |
| VPorod | 183 | nm3 |
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log I(s)
2.73×101
2.73×100
2.73×10-1
2.73×10-2
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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 PMCSASDHC5 – Nuclear factor kB p50/RelA heterodimer
Transcription factor p65 19-549NF-kappa-B p105 subunit 39-350
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Fits and models
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Synchrotron SAXS data from solutions of the nuclear factor kB p50/RelA heterodimer 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). Solute concentrations ranging between 2.5 and 5 mg/ml were measured at 10°C. 50 successive 15 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. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.
Storage temperature = UNKNOWN |
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