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Unless the targeted mesh is developable, metric distortion is inevitable during the process of surface mesh parameterization, thus one important objective of all involved parametric studies is to reduce the metric distortion. In order to further reduce area and angle distortion, a novel method of boundary-free mesh parameterization is presented in the paper. Firstly, the initial boundary-fixed conformal parameterization from 3D surface mesh patch to a plane is performed in the method. Then, based on the initial parameterization, the iterations of boundary-free quasi-harmonic parameterization are developed, where the tensor field is updated in each iterative step and the principal curvature direction is utilized to terminate the iteration. The solution of the novel method is convenient to calculate since it involves a series of linear systems. In our novel parameterization method, lower metric distortion and considerable efficiency have been obtained in experiments. [ABSTRACT FROM AUTHOR]

Protein-DNA interactions play important roles in regulations of many vital cellular processes, including transcription, translation, DNA replication and recombination. Sequence variants occurring in these DNA binding proteins that alter protein-DNA interactions may cause significant perturbations or complete abolishment of function, potentially leading to diseases. Developing a mechanistic understanding of impacts of variants on protein-DNA interactions becomes a persistent need. To address this need we introduce a new computational method PremPDI that predicts the effect of single missense mutation in the protein on the protein-DNA interaction and calculates the quantitative binding affinity change. The PremPDI method is based on molecular mechanics force fields and fast side-chain optimization algorithms with parameters optimized on experimental sets of 219 mutations from 49 protein-DNA complexes. PremPDI yields a very good agreement between predicted and experimental values with Pearson correlation coefficient of 0.71 and root-mean-square error of 0.86 kcal mol-1. The PremPDI server could map mutations on a structural protein-DNA complex, calculate the associated changes in binding affinity, determine the deleterious effect of a mutation, and produce a mutant structural model for download. PremPDI can be applied to many tasks, such as determination of potential damaging mutations in cancer and other diseases. PremPDI is available at . [ABSTRACT FROM AUTHOR]