Principal component analysis (PCA) is fundamental to statistical machine learning. It extracts latent principal factors that contribute to the most variation of the data. When data are stored across multiple machines, however, communication cost can prohibit the computation of PCA in a central location and distributed algorithms for PCA are thus needed. This paper proposes and studies a distributed PCA algorithm: each node machine computes the top K eigenvectors and transmits them to the central server; the central server then aggregates the information from all the node machines and conducts a PCA based on the aggregated information. We investigate the bias and variance for the resulting distributed estimator of the top K eigenvectors. In particular, we show that for distributions with symmetric innovation, the empirical top eigenspaces are unbiased, and hence the distributed PCA is unbiased. We derive the

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Current methods cannot tell us what the nature of the protein universe is concretely. They are based on different models of amino acid substitution and multiple sequence alignment which is an NP-hard problem and requires manual intervention. Protein structural analysis also gives a direction for mapping the protein universe. Unfortunately, now only a minuscule fraction of proteins' 3-dimensional structures are known. Furthermore, the phylogenetic tree representations are not unique for any existing tree construction methods. Here we develop a novel method to realize the nature of protein universe. We show the protein universe can be realized as a protein space in 60-dimensional Euclidean space using a distance based on a normalized distribution of amino acids. Every protein is in one-to-one correspondence with a point in protein space, where proteins with similar properties stay close together. Thus the distance between two points in protein space represents the biological distance of the corresponding two proteins. We also propose a natural graphical representation for inferring phylogenies. The representation is natural and unique based on the biological distances of proteins in protein space. This will solve the fundamental question of how proteins are distributed in the protein universe.

In this paper, we derive some local a priori estimates for the Ricci flow. This gives rise to some strong uniqueness theorems. As a corollary, let g(t) be a smooth complete solution to the Ricci flow on R3, with the canonical Euclidean metric E as initial data, then g(t) is trivial, i.e. g(t) ≡ E.

In this paper, we obtain some new Lyapunov-type inequalities for a class of even-order linear differential equations, the results are new and generalize and improve some early results in this field.