Site-selective ¹³C labeling of histidine and tryptophan using ribose.

ABSTRACT: Experimental studies on protein dynamics at atomic resolution by NMR-spectroscopy in solution require isolated ¹H-X spin pairs. This is the default scenario in standard ¹H-¹⁵N backbone experiments. Side chain dynamic experiments, which allow to study specific local processes like proton-transfer, or tautomerization, require isolated ¹H-¹³C sites which must be produced by site-selective ¹³C labeling. In the most general way this is achieved by using site-selectively ¹³C-enriched glucose as the carbon source in bacterial expression systems. Here we systematically investigate the use of site-selectively ¹³C-enriched ribose as a suitable precursor for ¹³C labeled histidines and tryptophans. The <

SUBMITTER: Weininger U 

PROVIDER: S-EPMC5626788 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature