투고논문

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.

Keywords NMR spectroscopy, ¹⁹F NMR, Hsp90, chaperone

* Address correspondence to: Jin Hae Kim, Department of New Biology, Daegu Gyeongbuk Institute of Science &Technology, Daegu 42988, Republic of Korea, Tel: 82-53-785-1770; E-mail: jinhaekim@dgist.ac.kr