Loïc Salmon

TL;DR: Flexible-meccano will be useful for researchers who wish to compare experimental data with those expected from a fully disordered protein, researchers who see experimental evidence of deviation from 'random coil' behaviour in their protein, or researchers who are interested in working with a broad ensemble of conformers representing the flexibility of the IDP of interest.

TL;DR: This study proposes a combination of paramagnetic relaxation enhancements (PREs) and residual dipolar couplings (RDCs) to define both long-range and local structural features of IDPs in solution, and demonstrates that ASTEROIDS, an ensemble selection algorithm, faithfully reproduces intramolecular contacts, even in the presence of highly diffuse, ill-defined target interactions.

TL;DR: This approach allows us to identify local conformational sampling properties of urea-unfolded ubiquitin, which shows that the backbone sampling of certain types of charged or polar amino acids is affected more strongly by urea binding than amino acids with hydrophobic side chains.

TL;DR: The model provides a structural framework for understanding the role of NTAIL in the initiation of viral transcription and replication, placing the flexible MoRE close to the viral RNA and, thus, positioning the polymerase complex in its functional environment.

TL;DR: An approach is developed, based on the combination of ensemble descriptions of unfolded proteins and state-of-the-art chemical shift prediction algorithms, to describe backbone dihedral angle conformational behavior on the basis of (13)C and (15)N NMR chemical shifts alone.