Solid-state 1H spin polarimetry by 13CH3 nuclear magnetic resonance

Abstract. Dissolution dynamic nuclear polarization is used to prepare nuclear spin polarizations approaching unity. At present, 1H polarization quantification in the solid state remains fastidious due to the requirement of measuring thermal equilibrium signals. Line shape polarimetry of solid-state nuclear magnetic resonance spectra is used to determine several useful properties regarding the spin system under investigation. In the case of highly polarized nuclear spins, such as those prepared under the conditions of dissolution dynamic nuclear polarization experiments, the absolute polarization of a particular isotopic species within the sample may be directly inferred from the characteristics of the corresponding resonance line shape. In situations where direct measurements of polarization are complicated by deleterious phenomena, indirect estimates of polarization using coupled heteronuclear spins prove informative. We present a simple analysis of the 13C spectral line shape of [2-13C]sodium acetate based on the normalized deviation of the centre of gravity of the 13C peaks, which can be used to indirectly evaluate the proton polarization of the methyl group moiety and very likely the entire sample in the case of rapid and homogeneous 1H–1H spin diffusion. For the case of positive microwave irradiation, 1H polarization was found to increase with an increasing normalized centre of gravity deviation. These results suggest that, as a dopant, [2-13C]sodium acetate could be used to indirectly gauge 1H polarizations in standard sample formulations, which is potentially advantageous for (i) samples polarized in commercial dissolution dynamic nuclear polarization devices that lack 1H radiofrequency hardware, (ii) measurements that are deleteriously influenced by radiation damping or complicated by the presence of large background signals and (iii) situations where the acquisition of a thermal equilibrium spectrum is not feasible. </jats:p

Extended Bloch-McConnell equations for mechanistic analysis of hyperpolarized 13C magnetic resonance experiments on enzyme systems

Abstract. We describe an approach to formulating the kinetic master equations of the time evolution of NMR signals in reacting (bio)chemical systems. Special focus is given to studies that employ signal enhancement (hyperpolarization) methods such as dissolution dynamic nuclear polarization (dDNP) and involving nuclear spin-bearing solutes that undergo reactions mediated by enzymes and membrane transport proteins. We extend the work given in a recent presentation on this topic to now include enzymes with two or more substrates and various enzyme reaction mechanisms as classified by Cleland. Using this approach, we can address some pressing questions in the field from a theoretical standpoint. For example, why does binding of a hyperpolarized substrate to an enzyme not cause an appreciable loss of the signal from the substrate or product? Why does the concentration of an unlabelled pool of substrate, for example 12C lactate, cause an increase in the rate of exchange of the 13C labelled pool? To what extent is the equilibrium position of the reaction perturbed during administration of the substrate? The formalism gives a full mechanistic understanding of the time courses derived and is of relevance to ongoing clinical trials using these techniques. </jats:p

Possible Applications of Dissolution Dynamic Nuclear Polarization in Conjunction with Zero- to Ultralow-Field Nuclear Magnetic Resonance

The combination of a powerful and broadly applicable nuclear hyperpolarization technique with emerging (near-)zero-field modalities offer novel opportunities in a broad range of nuclear magnetic resonance spectroscopy and imaging applications, including biomedical diagnostics, monitoring catalytic reactions within metal reactors and many others. These are discussed along with a roadmap for future developments.Comment: 12 pages, 5 figure

Current evidence shows no influence of women's menstrual cycle phase on acute strength performance or adaptations to resistance exercise training

Introduction: The bias towards excluding women from exercise science research is often due to the assumption that cyclical fluctuations in reproductive hormones influence resistance exercise performance and exercise-induced adaptations. Methods: Hence, the purpose of this umbrella review was to examine and critically evaluate the evidence from meta-analyses and systematic reviews on the influence of menstrual cycle phase on acute performance and chronic adaptations to resistance exercise training (RET). Results: We observed highly variable findings among the published reviews on the ostensible effects of female sex hormones on relevant RET-induced outcomes, including strength, exercise performance, and hypertrophy. Discussion: We highlight the importance of comprehensive menstrual cycle verification methods, as we noted a pattern of poor and inconsistent methodological practices in the literature. In our opinion, it is premature to conclude that short-term fluctuations in reproductive hormones appreciably influence acute exercise performance or longer-term strength or hypertrophic adaptations to RET

Perturbations of nuclear C*-algebras

Kadison and Kastler introduced a natural metric on the collection of all C*-subalgebras of the bounded operators on a separable Hilbert space. They conjectured that sufficiently close algebras are unitarily conjugate. We establish this conjecture when one algebra is separable and nuclear. We also consider one-sided versions of these notions, and we obtain embeddings from certain near inclusions involving separable nuclear C*-algebras. At the end of the paper we demonstrate how our methods lead to improved characterisations of some of the types of algebras that are of current interest in the classification programme.Comment: 45 page

X-Ray- and Neutron-Scattering Studies of α-Crystallin and Evidence That the Target Protein Sits in the Fenestrations of the α-Crystallin Shell

PURPOSE. α-Crystallin, a ubiquitous molecular chaperone, is found in high concentrations in the lens. Its structure and precise mechanism of action, however, are unknown. The purpose of these experiments was to further the understanding of the chaperone function of α-crystallin. METHODS. X-ray- and neutron-solution-scattering studies were used to measure the radius of gyration of bovine lens α-crystallin when complexed with its target protein β-crystallin in both normal and heavy-water-based solutions. Spectrophotometry was used as a chaperone assay. RESULTS. The radius of gyration of α-crystallin on its own and when mixed with β-crystallin was 69 ± 1 Å at 35°C and increased with the temperature. In contrast to H2O-buffered solutions, the radius of gyration did not increase significantly in D2O-buffered solutions up to 55°C, and at 70°C was, on average, some 15 to 20 Å smaller. CONCLUSIONS. Bovine lens α-crystallin in solution can be modeled as a fenestrated spherical shell of diameter 169 Å. At physiological temperatures, a weak interaction between α- and β-crystallin occurs, and β-crystallin is located in the fenestrations. Deuterium substitution indicates that the superaggregation process is controlled by hydrogen bonding. However, the chaperone process and superaggregation appear not to be linked