2,934 research outputs found

    amsrpm: Robust Point Matching for Retention Time Aligment of LC/MS Data with R

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    Proteomics is the study of the abundance, function and dynamics of all proteins present in a living organism, and mass spectrometry (MS) has become its most important tool due to its unmatched sensitivity, resolution and potential for high-throughput experimentation. A frequently used variant of mass spectrometry is coupled with liquid chromatography (LC) and is denoted as "LC/MS". It produces two-dimensional raw data, where significant distortions along one of the dimensions can occur between different runs on the same instrument, and between instruments. A compensation of these distortions is required to allow for comparisons between and inference based on different experiments. This article introduces the amsrpm software package. It implements a variant of the Robust Point Matching (RPM) algorithm that is tailored for the alignment of LC and LC/MS experiments. Problem-specific enhancements include a specialized dissimilarity measure, and means to enforce smoothness and monotonicity of the estimated transformation function. The algorithm does not rely on pre-specified landmarks, it is insensitive towards outliers and capable of modeling nonlinear distortions. Its usefulness is demonstrated using both simulated and experimental data. The software is available as an open source package for the statistical programming language R.

    Nanoscale Sensing Using Point Defects in Single-Crystal Diamond: Recent Progress on Nitrogen Vacancy Center-Based Sensors

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    Individual, luminescent point defects in solids so called color centers are atomic-sized quantum systems enabling sensing and imaging with nanoscale spatial resolution. In this overview, we introduce nanoscale sensing based on individual nitrogen vacancy (NV) centers in diamond. We discuss two central challenges of the field: First, the creation of highly-coherent, shallow NV centers less than 10 nm below the surface of single-crystal diamond. Second, the fabrication of tip-like photonic nanostructures that enable efficient fluorescence collection and can be used for scanning probe imaging based on color centers with nanoscale resolution.Comment: Overview paper on sensing with defects in diamond, we focus on creation of shallow NV centers and nanostructures, Final Version published in Crystal

    Tracking Cell Signals in Fluorescent Images

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    In this paper we present the techniques for tracking cell signal in GFP (Green Fluorescent Protein) images of growing cell colonies. We use such tracking for both data extraction and dynamic modeling of intracellular processes. The techniques are based on optimization of energy functions, which simultaneously determines cell correspondences, while estimating the mapping functions. In addition to spatial mappings such as affine and Thin-Plate Spline mapping, the cell growth and cell division histories must be estimated as well. Different levels of joint optimization are discussed. The most unusual tracking feature addressed in this paper is the possibility of one-to-two correspondences caused by cell division. A novel extended softassign algorithm for solutions of one-to-many correspondences is detailed in this paper. The techniques are demonstrated on three sets of data: growing bacillus Subtillus and e-coli colonies and a developing plant shoot apical meristem. The techniques are currently used by biologists for data extraction and hypothesis formation

    Revealing divergent evolution, identifying circular permutations and detecting active-sites by protein structure comparison

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    BACKGROUND: Protein structure comparison is one of the most important problems in computational biology and plays a key role in protein structure prediction, fold family classification, motif finding, phylogenetic tree reconstruction and protein docking. RESULTS: We propose a novel method to compare the protein structures in an accurate and efficient manner. Such a method can be used to not only reveal divergent evolution, but also identify circular permutations and further detect active-sites. Specifically, we define the structure alignment as a multi-objective optimization problem, i.e., maximizing the number of aligned atoms and minimizing their root mean square distance. By controlling a single distance-related parameter, theoretically we can obtain a variety of optimal alignments corresponding to different optimal matching patterns, i.e., from a large matching portion to a small matching portion. The number of variables in our algorithm increases with the number of atoms of protein pairs in almost a linear manner. In addition to solid theoretical background, numerical experiments demonstrated significant improvement of our approach over the existing methods in terms of quality and efficiency. In particular, we show that divergent evolution, circular permutations and active-sites (or structural motifs) can be identified by our method. The software SAMO is available upon request from the authors, or from and . CONCLUSION: A novel formulation is proposed to accurately align protein structures in the framework of multi-objective optimization, based on a sequence order-independent strategy. A fast and accurate algorithm based on the bipartite matching algorithm is developed by exploiting the special features. Convergence of computation is shown in experiments and is also theoretically proven
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