NIH R01 · 2025
Probing conformational changes by protein surface azidation
PROJECT SUMMARY Despite the rapid emergence of biophysical tools to detect and characterize conformational changes in protein structure, studying protein dynamics with high sensitivity and reliability in its native environment remains a formidable challenge. Laborious sample preparation and requirement for special equipment present a major obstacle for democratizing these tools. Thus, a simple yet robust platform for characterizing dynamic changes in protein conformation is highly demanded. Using azide-containing hypervalent iodine reagents, we have developed a novel chemoproteomic platform termed Protein Surface Azidation Mass Spectrometry (ProSurA-MS) that detects conformational changes…
From the public funding record at NIH RePORTER. Describes the funded project, not the reviews below.