A complete set of cross-correlated relaxation experiments for determining the protein backbone dihedral angles.

ABSTRACT: The investigation of structural propensities of proteins is essential for understanding how they function at the molecular level. NMR, offering atomic-scale information, is often the method of choice. One of the available techniques relies on the cross-correlated relaxation (CCR) effect, whose magnitude is related to local spatial conformation. Application of these methods is difficult if the protein under investigation exhibits high mobility, because NMR observables like CCR rates and chemical shifts present themselves as mere averages of an underlying ensemble distribution. Furthermore, relaxation observables are a convolution of structural and dynamical components. Despite these challenges, it is possible to infer the underlying structural ensemble by combining information from several

SUBMITTER: Bartosinska-Marzec P 

PROVIDER: S-EPMC12078423 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature