Conserved allosteric ensembles in disordered proteins using TROSY/anti-TROSY R₂-filtered spectroscopy.

ABSTRACT: Defining the role of intrinsic disorder in proteins in the myriad of biological processes with which it is involved represents a significant goal in modern biophysics. Toward this end, NMR is uniquely suited for molecular studies of dynamic and disordered regions, but studying these regions in concert with their more structured domains and binding partners presents spectroscopic challenges. Here, we investigate the interactions between the structured and disordered regions of the human glucocorticoid receptor (GR). To do this, we developed an NMR strategy that relies on a novel relaxation filter for the simultaneous study of structured and unstructured regions. Using this approach, we conducted a comparative analysis of three translational isoforms of GR containing a folded DNA-binding dom

SUBMITTER: Grasso EM 

PROVIDER: S-EPMC8390865 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature