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.

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We establish sharp asymptotics for the$L$^{$p$}-norm of Hermite polynomials and prove convergence in distribution of suitably normalized Wick powers. The results are combined with numerical integration to study an extremal problem on Wiener chaos.

We investigate the Kähler-Ricci flow on holomorphic fiber spaces whose generic fiber is a Calabi-Yau manifold. We establish uniform metric convergence to a metric on the base, away from the singular fibers, and show that the rescaled metrics on the fibers converge to Ricci-flat Kähler metrics. This strengthens previous work of Song-Tian and others. We obtain analogous results for degenerations of Ricci-flat Kähler metrics.

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