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The positivity-preserving property is an important and challenging issue for the numerical solution of radiative transfer equations. In the past few decades, different numerical techniques have been proposed to guarantee positivity of the radiative intensity in several schemes, however it is difficult to maintain both high order accuracy and positivity. The discontinuous Galerkin (DG) finite element method is a high order numerical method which is widely used to solve the neutron/photon transfer equations, due to its distinguished advantages such as high order accuracy, geometric flexibility, suitability for $h$- and $p$-adaptivity, parallel efficiency, and a good theoretical foundation for stability and error estimates. In this paper, we construct arbitrarily high order accurate DG schemes which preserve positivity of the radiative intensity in the simulation of both steady and unsteady radiative transfer equations in one- and two-dimensional geometry by using a combined technique of the scaling positivity-preserving limiter in \cite{ZS2} and a new rotational positivity-preserving limiter. This combined limiter is simple to implement and we prove the properties of positivity-preserving and high order accuracy rigorously. One- and two-dimensional numerical results are provided to verify the good properties of the positivity-preserving DG schemes.

In the present paper we prove that Hall polynomial exists for each triple of decomposition sequences which parameterize isomorphism classes of coherent sheaves of a domestic weighted projective line $\mathbb X$ over finite fields. These polynomials are then used to define the generic Ringel--Hall algebra of $\mathbb X$ as well as its Drinfeld double. Combining this construction with a result of Cramer, we show that Hall polynomials exist for tame quivers, which not only refines a result of Hubery, but also confirms a conjecture of Berenstein and Greenstein.

Structures and functions of proteins play various essential roles in biological processes. The functions of newly discovered proteins can be predicted by comparing their structures with that of known functional proteins. Many approaches have been proposed for measuring the protein structure similarity, such as the template-modeling (TM)-score method, GRaphlet (GR)-Align method as well as the commonly used root-mean-square deviation (RMSD) measures. However, the alignment comparisons between the similarity of protein structure cost much time on large dataset, and the accuracy still have room to improve. In this study, we introduce a new three-dimensional (3D) Yau–Hausdorff distance between any two 3D objects. The (3D) Yau–Hausdorff distance can be used in particular to measure the similarity/dissimilarity of two proteins of any size and does not need aligning and super- imposing two structures. We apply structural similarity to study function similarity and perform phylogenetic analysis on several datasets. The results show that (3D) Yau–Hausdorff distance could serve as a more precise and effective method to discover biological relationships between proteins than other methods on structure comparison.

We investigate meromorphic quasi-modular forms and their L-functions. We study the space of meromorphic quasi-modular forms and Rankin–Cohen brackets of meromorphic modular forms. Then we define their L-functions by using multiple techniques of regularized integral. Explicit formulas for the L-functions are given.