Recent advances in biomolecular 19F-NMR: applications to structural characterization of Hsp90
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Hsp90 is a dynamic chaperone protein whose ATP-driven conformational cycle plays critical roles in the maturation and regulation of client proteins. Due to its large size and multi-domain architecture, however, conventional structural methods provide only limited insight into its dynamic features and related functionalities. Recent advances in 19F NMR spectroscopy have enabled residue-specific and background-free monitoring of Hsp90 dynamics across multiple structural scales. This mini-review highlights three representative studies that employed 19F NMR to dissect Hsp90’s mechanistic cycle. These studies demonstrate the unique power of 19F NMR to probe conformational populations, exchange kinetics, and allosteric regulation in large protein systems.
Abstract
Hsp90 is a dynamic chaperone protein whose ATP-driven conformational cycle plays critical roles in the maturation and regulation of client proteins. Due to its large size and multi-domain architecture, however, conventional structural methods provide only limited insight into its dynamic features and related functionalities. Recent advances in 19F NMR spectroscopy have enabled residue-specific and background-free monitoring of Hsp90 dynamics across multiple structural scales. This mini-review highlights three representative studies that employed 19F NMR to dissect Hsp90’s mechanistic cycle. These studies demonstrate the unique power of 19F NMR to probe conformational populations, exchange kinetics, and allosteric regulation in large protein systems.