An analysis of factors affecting the market price of electricity: the case of Phelix index

The addition reaction of potassium atoms with oxygen has been studied using the collinear photofragmentation and atomic absorption spectroscopy (CPFAAS) method. KCl vapor was photolyzed with 266 nm pulses and the absorbance by K atoms at 766.5 nm was measured at various delay times with a narrow line width diode laser. Experiments were carried out with O₂/N₂ mixtures at a total pressure of 1 bar, over 748–1323 K. At the lower temperatures single exponential decays of [K] yielded the third-order rate constant for addition, <i>k</i>_R1, whereas at higher temperatures equilibration was observed in the form of double exponential decays of [K], which yielded both <i>k</i>_R1 and the equilibrium constant for KO₂ formation. <i>k</i>_R1 can be summarized as 1.07 × 10^–30(<i>T</i>/1000 K)^−0.733 cm⁶ molecule^–2 s^–1. Combination with literature values leads to a recommended <i>k</i>_R1 of 5.5 × 10^–26<i>T</i>^–1.55 exp­(−10/<i>T</i>) cm⁶ molecule^–2 s^–1 over 250–1320 K, with an error limit of a factor of 1.5. A van’t Hoff analysis constrained to fit the computed Δ<i>S</i>₂₉₈ yields a K–O₂ bond dissociation enthalpy of 184.2 ± 4.0 kJ mol^–1 at 298 K and Δ_f<i>H</i>₂₉₈(KO₂) = −95.2 ± 4.1 kJ mol^–1. The corresponding <i>D</i>₀ is 181.5 ± 4.0 kJ mol^–1. This value compares well with a CCSD­(T) extrapolation to the complete basis set limit, with all electrons correlated, of 177.9 kJ mol^–1

Proteomics-Based Methods for Discovery, Quantification, and Validation of Protein–Protein Interactions

Proteins play a fundamental role in establishing the diversity of cellular processes in health or disease systems. This diversity is accomplished by a vast array of protein functions. In fact, a protein rarely has a single function. The majority of proteins are involved in numerous cellular processes, and these multiple functions are made possible by interactions with other molecules. The complexity of interactions is substantially increased by the spatial and temporal diversity of proteins. For example, proteins can be part of distinct complexes within different subcellular compartments or at different stages of the cell cycle. Post-translational modifications can regulate and further expand the ability of proteins to establish localization- or temporal-dependent interactions. This complexity and functional divergence of interactions is further increased by the simultaneous presence of stable, transient, direct, and indirect protein interactions. Thus, an understanding of protein functions cannot be fully accomplished without knowledge of its interactions. Characterizing these interactions is therefore critical to understanding the biology of health and disease systems