DL-Histidine-[ring-15N2]

DL-Histidine-[ring-15N2], an isotopically labeled amino acid containing a stable nitrogen isotope, finds diverse applications in research. Here are key applications of DL-Histidine-[ring-15N2] presented with high perplexity and burstiness:

Metabolic Tracing: In metabolic studies, DL-Histidine-[ring-15N2] serves as a vital tool for tracing nitrogen pathways within organisms. By integrating this labeled amino acid into metabolic experiments, researchers can meticulously follow nitrogen flow and turnover, yielding profound insights into amino acid metabolism and nitrogen balance. This technique proves invaluable in elucidating protein synthesis and degradation dynamics in complex biological systems.

NMR Spectroscopy: Leveraging the nitrogen-15 isotope in DL-Histidine-[ring-15N2], researchers harness its potential as a key probe for nuclear magnetic resonance (NMR) spectroscopy investigations. This labeled compound enables the detailed examination of protein structure, dynamics, and interactions at a molecular level. The isotopic labeling significantly enhances signal sensitivity and resolution in NMR, furnishing researchers with intricate structural details essential for advancing their understanding of biological processes.

Protein Labeling: DL-Histidine-[ring-15N2] plays a pivotal role in incorporating isotopic labels into proteins for mass spectrometry analysis. By tagging proteins with nitrogen-15, researchers can easily differentiate them from their natural counterparts, facilitating precise mass spectrometry-based quantification and identification of post-translational modifications. This application holds paramount importance in the realm of proteomics research and biomarker discovery, driving breakthroughs in understanding complex biological systems.

Enzyme Mechanism Studies: Scientists utilize DL-Histidine-[ring-15N2] to delve into the intricate details of enzyme-catalyzed reactions, particularly those involving nitrogen-containing substrates. The isotopically labeled histidine enables researchers to trace reaction intermediates and scrutinize enzyme kinetics with precision. This approach plays a crucial role in unraveling the mechanisms of nitrogen transfer and shedding light on the functions of histidine residues within enzyme active sites, enriching our knowledge of enzymatic processes.