PubMed · 6016953
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I M Klotz. 1967-02-10. Protein subunits: a table.. https://doi.org/10.1126/science.155.3763.697
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NMR spin relaxation techniques that utilize relaxation interference phenomena (TROSY) enable chemical exchange processes to be characterized in high-molecular-weight proteins. A TROSY-selected (TS) approach for measuring off-resonance R1rho relaxation in the spin-locked rotating reference frame is developed using three principles: (i) deuteration of nonexchangeable 1H sites to minimize remote dipole-dipole interactions, (ii) selective excitation of the slowly relaxing 15N doublet component to obtain optimal initial conditions, and (iii) selective inversion of one of the 15N doublet components to suppress cross-relaxation during the spin-lock period. The method is validated using [90%-15N, 70%-2H] ubiquitin at 280 K. The TROSY-selected R1rho experiment enables characterization of backbone dynamics on the microsecond time scale in large proteins.
Pasture vegetation plays an important role in the air-surface exchange and food chain transfer of polycyclic aromatic hydrocarbons (PAHs). Therefore, considerable research has been focused towards measuring PAHs in vegetation using different analytical methods. However, in most cases information on the efficiencies of the different extraction methods employed is missing. This complicates data interpretation and inter-study comparisons. To address this deficiency, the extraction efficiencies of two commonly used pasture vegetation extraction techniques (sonication and soxhlet) and different solvents (hexane, DCM and hexane:acetone [4:1, v/v]) were compared. The completeness of the extraction was investigated using alkaline saponification in methanol. Soxhlet extraction was able to access between 60 and 90% of the total amount of PAHs in the pasture vegetation. Sonication was less efficient, only being able to extract between 10 and 50% of the PAHs. Extraction efficiencies were found to increase with increasing PAH molecular weight. The implications of these findings on data interpretation are discussed.
The orbitrap mass analyzer is proving itself as a useful addition to a proteomics tool box. The key attributes of this analyzer are accurate mass and high resolution similar to those achievable with FT ICR instrumentation. The basic principles underlying these capabilities, and how they translate into benefits in real-life proteomics experiments are discussed. The focus is on reviewing examples of protein identification with bottom-up and top-down approaches, and detection of post-translational modifications.