Investigating Water Accessibility in GB1 Protein Using Solid-state NMR at Fast Magic Angle Spinning

Investigating Water Accessibility in GB1 Protein Using Solid-state NMR at Fast Magic Angle Spinning

Chemistry

Eshana Samarakoon

2025

Józef R. Lewandowski, Todd Davey, Jairah Lubay

Solid-state NMR spectroscopy is a method that has been used to probe water accessibility in biological molecules. Water accessibility is the exposure of a biological structure to nearby water molecules. The interaction of water with proteins is essential for their structure and function, affecting protein folding and dynamics. Hence, applicability of the method is tested on a well-documented and simple model GB1 protein, which is a β1 immunoglobulin G-binding protein G derived from the streptococcus bacteria. The method employs fast magic-angle spinning (MAS) of the sample at 54.7° to average out anisotropic interactions and reduce line broadening. At 60 kHz, spin diffusion is partially suppressed so that a combination of spin diffusion and nuclear Overhauser effect (NOE) is responsible for polarization transfer.

Solid-state NMR, structural biology, chemistry, proteins