Whole Ribosome NMR: Dipolar Couplings and Contributions to Whole Cells.

ABSTRACT: Solid-state NMR is a powerful tool for quantifying chemical composition and structure in complex assemblies and even whole cells. We employed N{P} REDOR NMR to obtain atomic-level distance propensities in intact ¹⁵N-labeled E. coli ribosomes. The experimental REDOR dephasing of shift-resolved lysyl amine nitrogens by phosphorus was comparable to that expected from a calculation of N-P distances involving the lysines included in the crystal structure coordinates. Among the nitrogen contributions to the REDOR spectra, the strongest dephasing emerged from the dipolar couplings to phosphorus involving nitrogen peaks ascribed primarily to rRNA, and the weakest dephasing arose from protein amide nitrogens. This approach is applicable to any macromolecular system and provides quantitat

SUBMITTER: Nygaard R 

PROVIDER: S-EPMC5897578 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature