Determination of the Molecular Interactions of Bovine Gamma B Crystallins Using NMR Spectroscopy

Le résumé fourni par la source

Crystallins are proteins found in the eye and are responsible for regulating the transparency of the lens. Interactions between crystallins can cause phase separation and aggregation, which can decrease lens clarity and disrupt vision by causing cataracts. To study the orientation‐dependent interactions between crystallins, we utilized recombinant bovine γ‐B crystallin (CRYGB) proteins expressed in Escherichia coli . We acquired nuclear magnetic resonance (NMR) spectra on 15 N/ 13 C labeled CRYGB and completed the backbone residue assignments. Standard triple‐resonance spectra were acquired at NMR Facility at Madison (NMRFAM) on 600, 800, and 900 MHz spectrometers. HSQC experiments at variable concentrations revealed subtle chemical shift perturbations that, we propose, are the result of CRYGB interactions. Overall rotational correlation times (τ c) and translational diffusion rates demonstrated the concentration and temperature dependences on protein diffusion times. Preliminary results suggest that the sensitivity of NMR allows for a detailed look at how CRYGB proteins interact.

Ce résumé expose les affirmations des auteurs. BNTIC ne l’interprète pas comme une validation indépendante des résultats.