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Integrating smFRET, SAXS and NMR data to infer structural ensembles of an intrinsically-disordered protein
[article]
2020
bioRxiv
pre-print
Intrinsically disordered proteins (IDPs) have fluctuating heterogeneous conformations, which makes structural characterization challenging. Transient long-range interactions in IDPs are known to have important functional implications. Thus, in order to calculate reliable structural ensembles of IDPs, the data used in their calculation must capture these important structural features. We use integrative modelling to understand and implement conformational restraints imposed by the most common
doi:10.1101/2020.02.05.935890
fatcat:sxphuktwnndknbyjrnugbyor74