太阳风等离子体输出流量的全日面二维结构

本文根据1983年十个 Carrington 周(1733—1742)期间的 K-日冕亮度、行星际闪烁(IPS)观测和光球磁场观测,首次探讨了太阳风等离子体质量、动量和能量输出流量 F_M,F_P 和 F_E 的全日面二维平均结构及其与光球磁场结构的关系.     

Excited states in126Ba

The K=3/2 ₁ ^T rotational band has been identified in⁹⁹Y with a band-head energy of 536 keV. This result is in contradiction with previously reported data, but is in agreement with predictions of the IBFM/PTQM model.     

Quantum fog and the degradation of information by the gravitational field

In this paper we discuss how information transferred optically through a gravitational field is degraded as the quanta interact with the madium (vacuum state). We quantify information by means of Shannon's entropy, and consider information carriers that are quanta of some field. Next, we obtain the quantum noise (quantum fog) produced by the gravitational field and derive the appropriate channel capacity formula, which quantifies the maximum amount of information that can be transmitted per pulse, in the face of this noise. We show that the channel capacity formula vanishes if the source of information is a space-time singularity because a very intense noise is produced in the vicinity of the singularity. In other words, space-time singularities are hidden behind a very intense quantum fog and cannot be optically observed. A second consequence is that information is degraded as anisotropies (lumpiness) develop in the universe.     

Proton uptake of rhodobacter capsulatus reaction center mutants modified in the primary quinone environment

Flash-induced absorbance spectroscopy was used to analyze the proton uptake and electron transfer properties of photosynthetic reaction centers (RC) of Rhodobacter capsulatus that have been genetically modified near the primary quinone electron acceptor (Q(A)). M246Ala and M247Ala, which are symmetry-related to the positions of two acidic groups, L212Glu and L213Asp, in the secondary quinone electron acceptor (QB) protein environment, have been mutated to Glu and Asp, respectively. The pH dependence of the stoichiometry of proton uptake upon formation of the P+Q(A)- (H+/P+Q(A)-) and PQ(A) (H+/Q(A)-) (P is the primary electron donor, a noncovalently linked bacteriochlorophyll dimer) states have been measured in the M246Ala --> Glu and the M247Ala --> Asp mutant RC, in the M246Ala-M247Ala --> Glu-Asp double mutant and in the wild type (WT). Our results show that the introduction of an acidic group (Glu or Asp) in the QA protein region induces notable additional proton uptake over a large pH region (approximately 6-9), which reflects a delocalized response of the protein to the formation of Q(A)-. This may indicate the existence of a widely spread proton reservoir in the cytoplasmic region of the protein. Interestingly, the pH titration curves of the proton release caused by the formation of P+ (H+/P+: difference between H+/P+Q(A)- and H+/PQ(A)- curves) are nearly superimposable in the WT and the M246Ala --> Glu mutant RC, but substantial additional proton release is detected between pH 7 and 9 in the M247Ala --> Asp mutant RC. This effect can be accounted for by an increased proton release by the P+ environment in the M247Ala --> Asp mutant. The M247Ala --> Asp mutation reveals the existence of an energetic and conformational coupling between donor and acceptor sides of the RC at a distance of nearly 30A.     

Gyromagnetic ratios of low-lying rotational states in156, 158, 160Gd

Transient-field precessions were measured simultaneously for levels in the ground-state bands of^{156, 158, 160}Gd as ions of these nuclei traversed a thin polarized Fe foil. Relative g-factors of levels up to 6 ₁ ⁺ were deduced, those of the 4 ₁ ⁺ levels being determined with greatest precision. In contrast with the conclusions of the recent report by Alzner et al. [1], our results are consistent with g(4 ₁ ⁺ ) having the same value in all three isotopes and imply g(2 ₁ ⁺ )=g(4 ₁ ⁺ ) in¹⁵⁶Gd, consistent with nuclear structure models.