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Abstract:

<jats:title>ABSTRACT</jats:title> <jats:p>A key challenge in the search for primordial B-modes is the presence of polarized Galactic foregrounds, especially thermal dust emission. Power-spectrum-based analysis methods generally assume the foregrounds to be Gaussian random fields when constructing a likelihood and computing the covariance matrix. In this paper, we investigate how non-Gaussianity in the dust field instead affects CMB and foreground parameter inference in the context of inflationary B-mode searches, capturing this effect via modifications to the dust power-spectrum covariance matrix. For upcoming experiments such as the Simons Observatory, we find no dependence of the tensor-to-scalar ratio uncertainty $\sigma (r)$ on the degree of dust non-Gaussianity or the nature of the dust covariance matrix. We provide an explanation of this result, noting that when frequency decorrelation is negligible, dust in mid-frequency channels is cleaned using high-frequency data in a way that is independent of the spatial statistics of dust. We show that our results hold also for non-zero levels of frequency decorrelation that are compatible with existing data. We find, however, that neglecting the impact of dust non-Gaussianity in the covariance matrix can lead to inaccuracies in goodness-of-fit metrics. Care must thus be taken when using such metrics to test B-mode spectra and models, although we show that any such problems can be mitigated by using only cleaned spectrum combinations when computing goodness-of-fit statistics.</jats:p>

Abstract:

F₁F_o ATP synthase functions as a biological generator and makes a major contribution to cellular energy production. Proton flow generates rotation in the F_o motor that is transferred to the F₁ motor to catalyze ATP production, with flexible F₁/F_o coupling required for efficient catalysis. F₁F_o ATP synthase can also operate in reverse, hydrolyzing ATP and pumping protons, and in bacteria this function can be regulated by an inhibitory ε subunit. Here we present cryo-EM data showing E. coli F₁F_o ATP synthase in different rotational and inhibited sub-states, observed following incubation with 10 mM MgATP. Our structures demonstrate how structural transitions within the inhibitory ε subunit induce torsional movement in the central stalk, thereby enabling its rotation within the F_ο motor. This highlights the importance of the central rotor for flexible coupling of the F₁ and F_o motors and provides further insight into the regulatory mechanism mediated by subunit ε.