Phospholipids in Motion: High-Resolution P NMR Field Cycling Studies.

Diverse phospholipid motions are key to membrane function but can be quite difficult to untangle and quantify. High-resolution field cycling P NMR spin-lattice relaxometry, where the sample is excited at high field, shuttled in the magnet bore for low-field relaxation, then shuttled back to high field for readout of the residual magnetization, provides data on phospholipid dynamics and structure. This information is encoded in the field dependence of the P spin-lattice relaxation rate ().

Enzyme-Substrate-Cofactor Dynamical Networks Revealed by High-Resolution Field Cycling Relaxometry.

The remarkable power and specificity of enzyme catalysis rely on the dynamic alignment of the enzyme, substrates, and cofactors, yet the role of dynamics has usually been approached from the perspective of the protein. We have been using an underappreciated NMR technique, subtesla high-resolution field cycling P NMR relaxometry, to investigate the dynamics of the enzyme-bound substrates and cofactor on guanosine-5'-monophosphate reductase (GMPR). GMPR forms two dead end, yet catalytically competent, complexes that mimic distinct steps in the catalytic cycle: E·IMP·NADP undergoes a partial hydride transfer reaction, while E·GMP·NADP undergoes a partial deamination reaction.

Dynamic Characteristics of Guanosine-5'-monophosphate Reductase Complexes Revealed by High-Resolution P Field-Cycling NMR Relaxometry.

The ability of enzymes to modulate the dynamics of bound substrates and cofactors is a critical feature of catalysis, but the role of dynamics has largely been approached from the perspective of the protein. Here, we use an underappreciated NMR technique, subtesla high-resolution field-cycling P NMR relaxometry, to interrogate the dynamics of enzyme bound substrates and cofactors in guanosine-5'-monophosphate reductase (GMPR). These experiments reveal distinct binding modes and dynamic profiles associated with the P nuclei in the Michaelis complexes for the deamination and hydride transfer steps of the catalytic cycle.

Substrate and Cofactor Dynamics on Guanosine Monophosphate Reductase Probed by High Resolution Field Cycling 31P NMR Relaxometry.

Guanosine-5'-monophosphate reductase (GMPR) catalyzes the reduction of GMP to IMP and ammonia with concomitant oxidation of NADPH. Here we investigated the structure and dynamics of enzyme-bound substrates and cofactors by measuring P relaxation rates over a large magnetic field range using high resolution field cycling NMR relaxometry. Surprisingly, these experiments reveal differences in the low field relaxation profiles for the monophosphate of GMP compared with IMP in their respective NADP complexes.

Effects of conventional and alternative curing methods on processed turkey quality traits.

Deli-style turkey breast cured with pre-converted celery juice powder (CP) or sodium nitrite (SN) was manufactured with ingoing SN concentrations or equivalent of 0, 50, 100, 150, and 200 ppm. Cured and total meat pigment, salt, and water activity were measured on d 0; color, pH, and residual nitrite were measured on d 0, 7, 14, 21, 28, 35, and 42. Untrained panelists evaluated sensory traits of 50, 100, 150, and 200 ppm products.