Surface parameterizations have been widely applied to digital geometry processing. In this paper, we propose an efficient conformal energy minimization (CEM) algorithm for computing conformal parameterizations of simply-connected open surfaces with a very small angular distortion and a highly improved computational efficiency. In addition, we generalize the proposed CEM algorithm to computing conformal parameterizations of multiply-connected surfaces. Furthermore, we prove the existence of a nontrivial accumulation point of the proposed CEM algorithm under some mild conditions. Several numerical results show the efficiency and robustness of the CEM algorithm comparing to the existing state-of-the-art algorithms. An application of the CEM on the surface morphing between simply-connected open surfaces is demonstrated thereafter. Thanks to the CEM algorithm, the whole computations for the surface morphing can be performed efficiently and robustly.

A multilevel quality-guided phase unwrapping algorithm for real-time 3D shape measurement is presented. The quality map is generated from the gradient of the phase map. Multilevel thresholds are used to unwrap the phase level by level. Within the data points in each level, a fast scan-line algorithm is employed. The processing time of this algorithm is approximately 18.3 ms for an image size of 640480 pixels in an ordinary computer. We demonstrate that this algorithm can be implemented into our real-time 3D shape measurement system for real-time 3D reconstruction. Experiments show that this algorithm improves the previous scan-line phase unwrapping algorithm significantly although it reduces its processing speed slightly.

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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 article we provide a proof of the Iitaka Cnm conjecture for algebraic fiber spaces over tori.