Side-chain-selective deuterium labeling by a simple bio-expression method enhances resolution and simplifies spectra in ¹H-detected protein solid-state NMR.

ABSTRACT: We present a novel approach for side-chain-selective deuteration of proteins to improve ¹H_α spectral resolution and to simplify side-chain signals in ¹H-detected protein solid-state NMR (SSNMR) with a simple bio-expression method using E. coli BL21 (DE3). ¹H-detected SSNMR using ultra-fast magic-angle spinning (MAS) at a spinning rate of 60 kHz or higher is attracting attention as a powerful method of protein structure determination. However, even with ultra-fast MAS at 100 kHz, the ¹H line broadening due to ¹H-¹H dipolar interactions cannot be eliminated, posing an obstacle to signal assignment and structure determination. To improve resolution for SSNMR-based protein structural analysis, we developed a method to

SUBMITTER: Shigemitsu Y 

PROVIDER: S-EPMC12664835 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature