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![[Figure 8]](/d/issues/2025/07/00/ag5054/ag5054fig8mag.jpg)
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| Figure 8 A cartoon model emphasizing the behaviour of SFPQ IDRs based on experimental results. (a) SEC-SAXS modelling and XL-MS indicate overlapping conformational space of the N- and C-terminal IDRs, meaning that an interaction between them is possible. (b) An additional shorter SANS P(r) function with a shoulder shows that this interaction is likely to become more pronounced at low salt concentrations. The interaction of the two IDRs is likely to serve to negatively regulate phase separation. The N-terminal IDR can collapse onto itself (c, d) in response to changing salt concentrations. This `stickiness' may be relevant for the recognition of dsDNA, which may occur in a more structured way where the N-terminal IDR folds upon binding dsDNA or for interactions with the nearby C-terminal IDR. (e) The binding of the N-terminal IDR to nucleic acids (long grey bar) would free the C-terminal IDR to drive LLPS. This may act as a trigger that promotes phase separation. |
![[Figure 8]](https://journals.iucr.org/10.1107/S2059798325005303/ag5054fig8.jpg)
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STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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