¹⁹F NMR-based solvent accessibility profiling reveals tryptophan ring-flip dynamics in a protein.

ABSTRACT: Aromatic ring flipping is a key component of protein conformational dynamics, particularly in facilitating breathing motions that involve cooperative rearrangements of hydrophobic cores. While phenylalanine and tyrosine flipping have been extensively studied, tryptophan flipping has often been overlooked due to assumptions about limited mobility arising from its bulkiness and the asymmetric structure of the indole ring. Here, we report a ¹⁹F NMR-based approach to probe the dynamic flipping of Trp23 in the DNA-binding domain (DBD) of heat shock factor 1 (Hsf1). We incorporated 5-fluorotryptophan into the Hsf1 DBD and monitored Trp23 flipping in solution using ¹⁹F NMR. Temperature-dependent analysis corroborated with relaxation dispersion experiments revealed interconve

SUBMITTER: Kawagoe S 

PROVIDER: S-EPMC12432518 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature