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![[Figure 5]](/d/issues/2025/07/00/ag5054/ag5054fig5mag.jpg)
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| Figure 5 SANS experiments indicating dimer partner exchange between SFPQ homodimers. (a) Log(I) versus log(q) plot for an experiment featuring ∼5% protiated SFPQ (hSFPQ) and 95% deuterated SFPQ (dSFPQ) at a D2O match-point of 95%. (b) Guinier plot for (a) indicating the qRg range of 0.74–1.25 with a Guinier Rg of 61.06 ± 3.55 Å. (c) Residual plot of the Guinier fit. (d) Log(I) versus log(q) plot for an experiment featuring ∼5% hSFPQ and 95% dSFPQ in H2O without any match-out. (e) Guinier plot for (d) indicating the qRg range of 0.71–1.27 with a Guinier Rg of 86.55 ± 4.29 Å. (f) Residual plot of the Guinier fit from (e). (g) A comparative P(r) function plot between full-length SFPQ as observed with SEC-SAXS and the SANS data from these experiments. Differing peak maxima, function shapes and Dmax values indicate that the blue curve corresponds to a monomer of full-length SFPQ. The differing maxima, Dmax values and overall changes in shape between the purple and grey functions may be evidence of the compaction of full-length SFPQ in different salt conditions. (h) DAMAVER (grey) and DAMFILT (blue) envelopes processed from the matched-out SANS data, with an atomistic model of a monomer of SFPQ including just the folded domain superposed over the envelope. This further confirms that the blue function in (g) corresponds to a monomer of SFPQ. |
![[Figure 5]](https://journals.iucr.org/10.1107/S2059798325005303/ag5054fig5.jpg)
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STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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