Dataset Information

Investigating Energetic X-Shaped Flares on the Outskirts of A Solar Active Region.

ABSTRACT: Typical solar flares display two quasi-parallel, bright ribbons on the chromosphere. In between is the polarity inversion line (PIL) separating concentrated magnetic fluxes of opposite polarity in active regions (ARs). Intriguingly a series of flares exhibiting X-shaped ribbons occurred at the similar location on the outskirts of NOAA AR 11967, where magnetic fluxes were scattered, yet three of them were alarmingly energetic. The X shape, whose center coincided with hard X-ray emission, was similar in UV/EUV, which cannot be accommodated in the standard flare model. Mapping out magnetic connectivities in potential fields, we found that the X morphology was dictated by the intersection of two quasi-separatrix layers, i.e., a hyperbolic flux tube (HFT), within which a separator connecting a double null was embedded. This topology was not purely local but regulated by fluxes and flows over the whole AR. The nonlinear force-free field model suggested the formation of a current layer at the HFT, where the current dissipation can be mapped to the X-shaped ribbons via field-aligned heat conduction. These results highlight the critical role of HFTs in 3D magnetic reconnection and have important implications for astrophysical and laboratory plasmas.

SUBMITTER: Liu R

PROVIDER: S-EPMC5039731 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

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Investigating Energetic X-Shaped Flares on the Outskirts of A Solar Active Region.

Liu Rui R Chen Jun J Wang Yuming Y Liu Kai K

Scientific reports 20160928

Typical solar flares display two quasi-parallel, bright ribbons on the chromosphere. In between is the polarity inversion line (PIL) separating concentrated magnetic fluxes of opposite polarity in active regions (ARs). Intriguingly a series of flares exhibiting X-shaped ribbons occurred at the similar location on the outskirts of NOAA AR 11967, where magnetic fluxes were scattered, yet three of them were alarmingly energetic. The X shape, whose center coincided with hard X-ray emission, was simi ...[more]

PMID: 27677354

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Project description:Accumulated experimental observations demonstrate that protein stability is often preserved upon conservative point mutation. In contrast, less is known about the effects of large sequence or structure changes on the stability of a particular fold. Almost completely unknown is the degree to which stability of different regions of a protein is generally preserved throughout evolution. In this work, these questions are addressed through thermodynamic analysis of a large representative sample of protein fold space based on remote, yet accepted, homology. More than 3,000 proteins were computationally analyzed using the structural-thermodynamic algorithm COREX/BEST. Estimated position-specific stability (i.e., local Gibbs free energy of folding) and its component enthalpy and entropy were quantitatively compared between all proteins in the sample according to all-vs.-all pairwise structural alignment. It was discovered that the local stabilities of homologous pairs were significantly more correlated than those of non-homologous pairs, indicating that local stability was indeed generally conserved throughout evolution. However, the position-specific enthalpy and entropy underlying stability were less correlated, suggesting that the overall regional stability of a protein was more important than the thermodynamic mechanism utilized to achieve that stability. Finally, two different types of statistically exceptional evolutionary structure-thermodynamic relationships were noted. First, many homologous proteins contained regions of similar thermodynamics despite localized structure change, suggesting a thermodynamic mechanism enabling evolutionary fold change. Second, some homologous proteins with extremely similar structures nonetheless exhibited different local stabilities, a phenomenon previously observed experimentally in this laboratory. These two observations, in conjunction with the principal conclusion that homologous proteins generally conserved local stability, may provide guidance for a future thermodynamically informed classification of protein homology.

Dataset Information

Investigating Energetic X-Shaped Flares on the Outskirts of A Solar Active Region.

Publications

Investigating Energetic X-Shaped Flares on the Outskirts of A Solar Active Region.

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