Rapid Interpretation of Protein Backbone Rotation Dynamics Directly from Spin Relaxation Data.

Besides their structure, dynamics is pivotal for protein functions, particularly for intrinsically disordered proteins (IDPs) that do not fold into a fixed 3D structure. However, the detection of protein dynamics is difficult for IDPs and other disordered biomolecules. NMR spin relaxation rates are sensitive to the rapid rotations of chemical bonds, but their interpretation is arduous for IDPs or molecular assemblies with a complex dynamic landscape.

Probing the dynamic landscape of peptides in molecular assemblies by synergized NMR experiments and MD simulations.

Peptides or proteins containing small biomolecular aggregates, such as micelles, bicelles, droplets and nanodiscs, are pivotal in many fields ranging from structural biology to pharmaceutics. Monitoring dynamics of such systems has been limited by the lack of experimental methods that could directly detect their fast (picosecond to nanosecond) timescale dynamics. Spin relaxation times from NMR experiments are sensitive to such motions, but their interpretation for biomolecular aggregates is not straightforward.

Impact on wine sales of removing the largest serving size by the glass: An A-B-A reversal trial in 21 pubs, bars, and restaurants in England.

Background: Interventions that alter aspects of the physical environments in which unhealthy behaviours occur have the potential to change behaviour at scale, i.e., across populations, and thereby decrease the risk of several diseases.