Conformational ensembles explain NMR spectra of frozen intrinsically disordered proteins
 

Conformational ensembles explain NMR spectra of frozen intrinsically disordered proteins

Protein regions, which are intrinsically disordered, exist as an ensemble of rapidly interconverting structures. Cooling proteins to cryogenic temperatures for DNP MAS NMR studies suspends most of the motions, resulting in peaks that are broad but not featureless. To demonstrate that detailed conformational restraints can be retrieved from the peak shapes of frozen proteins alone, we developed and used a simulation framework to assign peak features to conformers in the ensemble. We validated our...

More...