Dityrosine-[13C12]

Dityrosine-[13C12] is a compound labeled with stable isotopes, commonly utilized in cutting-edge scientific research. Here are key applications of Dityrosine-[13C12], presented with high degrees of perplexity and burstiness:

Protein Cross-Linking Studies: Acting as a pivotal marker in the exploration of protein cross-linking, Dityrosine-[13C12] stands out as an invaluable tool for unraveling the intricate structure and functionality of proteins. By introducing this labeled compound into protein samples, researchers can meticulously trace cross-linking occurrences and delve into alterations in protein complex assembly. This application plays a vital role in deciphering the mechanisms underlying protein aggregation in neurodegenerative diseases like Alzheimer’s and Parkinson’s.

Oxidative Stress Research: Delving into the realm of oxidative stress, Dityrosine-[13C12] emerges as a crucial biomarker utilized to gauge the extent of protein oxidation. Offering a precise means of detecting post-translational modifications arising from oxidative stress within cells, this compound enables researchers to deepen their understanding of cellular processes associated with aging and various diseases. This research avenue lays the groundwork for the development of antioxidant therapies aimed at mitigating oxidative damage.

Quantitative Proteomics: Positioned at the forefront of quantitative proteomics, Dityrosine-[13C12] plays a pivotal role in the measurement and comparison of protein levels within complex biological samples. Leveraging its stable isotope label, it serves as an internal standard, facilitating accurate protein quantitation via mass spectrometry. This technique is indispensable for identifying biomarkers and unraveling the dynamic interplay of proteins within cellular pathways, offering invaluable insights into biological processes at a molecular level.

Structural Biology: Within the realm of structural biology, Dityrosine-[13C12] serves as a cornerstone for investigating protein conformational changes and stability. By integrating the labeled dityrosine into protein structures, scientists can employ advanced techniques, such as NMR or mass spectrometry, to evaluate how environmental factors influence protein folding and integrity. Such in-depth studies form the bedrock of drug design efforts and contribute significantly to our understanding of disease-associated protein misfolding phenomena, pushing the boundaries of structural biology research.