We consider an elliptic pseudo-differential equation with a highly oscillating linear potential modeled as a stationary ergodic random field. The random field is a function composed with a centered long-range correlated Gaussian process. In the limiting of vanishing correlation length, the heterogeneous solution converges to a deterministic solution obtained by averaging the random potential. We characterize the deterministic and stochastic correctors. With proper rescaling, the mean-zero stochastic corrector converges to a Gaussian random process in probability and weakly in the spatial variables. In addition, for two prototype equations involving the Laplacian and the fractional Laplacian operators, we prove that the limit holds in distribution in some Hilbert spaces. We also determine the size of the deterministic corrector when it is larger than the stochastic corrector. Depending on the correlation structure of the random field and on the singularities of the Green’s function, we show that either the deterministic or the random part of the corrector dominates.

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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.

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The nuclear norm is widely used to induce low-rank solutions for many optimization problems with matrix variables. Recently, it has been shown that the augmented Lagrangian method (ALM) and the alternating direction method (ADM) are very efficient for many convex programming problems arising from various applications, provided that the resulting subproblems are sufficiently simple to have closed-form solutions. In this paper, we are interested in the application of the ALM and the ADM for some nuclear norm involved minimization problems. When the resulting subproblems do not have closed-form solutions, we propose to linearize these subproblems such that closed-form solutions of these linearized subproblems can be easily derived. Global convergence results of these linearized ALM and ADM are established under standard assumptions. Finally, we verify the effectiveness and efficiency of these new methods by some numerical experiments.