Measurement of protein backbone ¹³CO and ¹⁵N relaxation dispersion at high resolution.

ABSTRACT: Peak overlap in crowded regions of two-dimensional spectra prevents characterization of dynamics for many sites of interest in globular and intrinsically disordered proteins. We present new three-dimensional pulse sequences for measurement of Carr-Purcell-Meiboom-Gill relaxation dispersions at backbone nitrogen and carbonyl positions. To alleviate increase in the measurement time associated with the additional spectral dimension, we use non-uniform sampling in combination with two distinct methods of spectrum reconstruction: compressed sensing and co-processing with multi-dimensional decomposition. The new methodology was validated using disordered protein CD79A from B-cell receptor and an SH3 domain from Abp1p in exchange between its free form and bound to a peptide from the protein Ark1p

SUBMITTER: Mayzel M 

PROVIDER: S-EPMC5626786 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature