Residue-Specific High-Resolution ¹⁷O Solid-State Nuclear Magnetic Resonance of Peptides: Multidimensional Indirect ¹H Detection and Magic-Angle Spinning.

ABSTRACT: Oxygen is an integral component of proteins but remains sparsely studied because its only NMR active isotope, ¹⁷O, has low sensitivity, low resolution, and large quadrupolar couplings. These issues are addressed here with efficient isotopic labeling, high magnetic fields, fast sample spinning, and ¹H detection in conjunction with multidimensional experiments to observe oxygen sites specific to each amino acid residue. Notably, cross-polarization at high sample spinning frequencies provides efficient ¹³C ↔ ¹⁷O polarization transfer. The use of ¹⁷O for initial polarization is found to provide better sensitivity per unit time compared to ¹H. Sharp isotropic ¹⁷O peaks are obtained by using a low-power multiple-quantum

SUBMITTER: Hung I 

PROVIDER: S-EPMC9888599 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature