Local structure propensities in disordered proteins from cross-correlated NMR spin relaxation.

ABSTRACT: Structurally diverse ensembles of intrinsically disordered proteins or regions are difficult to determine, because experimental observables usually report a conformational average. Therefore, in order to infer the underlying distribution, a set of experiments that measure different aspects of the system is necessary. In principle, there exists a set of cross-correlated relaxation (CCR) rates that report on protein backbone geometry in a complementary way. However, CCR rates are hard to interpret, because geometric information is encoded in an ambiguous way and they present themselves as a convolute of both structure and dynamics. Despite these challenges, CCR rates analyzed within a suitable statistical framework are able to identify conformations in structured proteins. In the context of

SUBMITTER: Braun D 

PROVIDER: S-EPMC12078414 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature