Heidar Koning
@heidarkoning.bsky.social
PhD student in structural biology/musician 🧬🎸
Working on RNA-binding proteins, phase separation, and coiled coils with relevance to disease and mammalian gene regulation.
Google Scholar: https://scholar.google.com.au/citations?hl=en&user=xZrhsIoAAAAJ
Working on RNA-binding proteins, phase separation, and coiled coils with relevance to disease and mammalian gene regulation.
Google Scholar: https://scholar.google.com.au/citations?hl=en&user=xZrhsIoAAAAJ
Reposted by Heidar Koning
Our July issue is out tinyurl.com/2u2cj472
On the cover: structural studies of the intrinsically disordered regions of human SFPQ reveal that it is capable of swapping dimer partners with itself. Find out more at doi.org/10.1107/S205...
On the cover: structural studies of the intrinsically disordered regions of human SFPQ reveal that it is capable of swapping dimer partners with itself. Find out more at doi.org/10.1107/S205...
July 3, 2025 at 2:35 PM
Our July issue is out tinyurl.com/2u2cj472
On the cover: structural studies of the intrinsically disordered regions of human SFPQ reveal that it is capable of swapping dimer partners with itself. Find out more at doi.org/10.1107/S205...
On the cover: structural studies of the intrinsically disordered regions of human SFPQ reveal that it is capable of swapping dimer partners with itself. Find out more at doi.org/10.1107/S205...
Our SFPQ paper is out! 👌 If you're interested in disordered proteins, phase separation, SAXS/SANS, or mass spectrometry, give it a read 🧬
Heidar J. Koning et al.: Structural dynamics of IDR interactions in human SFPQ and implications for liquid–liquid phase separation ##PhaseSeparation##Disorder##Flexibility@uwanews@unimelb...##IUCrhttps://journals.iucr.org/paper?S2059798325005303
Structural dynamics of IDR interactions in human SFPQ and implications for liquid–liquid phase separation
SFPQ and NONO are DBHS-family proteins that are essential for transcriptional regulation and the assembly of paraspeckles, which are subnuclear structures built on the long noncoding RNA NEAT1. Through SAXS, SANS and XL-MS analyses, we reveal that the disordered regions of SFPQ surrounding its DBHS domain enable flexible interactions and that the full-length proteins are capable of dimer partner exchange, highlighting how these dynamics may contribute to phase separation and impact disease processes.
journals.iucr.org
June 28, 2025 at 1:59 AM
Our SFPQ paper is out! 👌 If you're interested in disordered proteins, phase separation, SAXS/SANS, or mass spectrometry, give it a read 🧬