1,722,457 research outputs found
W.J. and Ruby Moad
W.J. Moad and his wife Ruby Emma Cavender Moad, daughter of J.M. Cavende
MOAD: Modeling Observation-based Approximate Dependency
While dependency analysis is foundational to many applications of program analysis, the static nature of many existing techniques presents challenges such as limited scalability and inability to cope with multi-lingual systems. We present a novel dependency analysis technique that aims to approximate program dependency from a relatively small number of perturbed executions. Our technique, called MOAD (Modeling Observation-based Approximate Dependency), reformulates program dependency as the likelihood that one program element is dependent on another, instead of a more classical Boolean relationship. MOAD generates a set of program variants by deleting parts of the source code, and executes them while observing the impacts of the deletions on various program points. From these observations, MOAD infers a model of program dependency that captures the dependency relationship between the modification and observation points. While MOAD is a purely dynamic dependency analysis technique similar to Observation Based Slicing (ORBS), it does not require iterative deletions. Rather, MOAD makes a much smaller number of multiple, independent observations in parallel and infers dependency relationships for multiple program elements simultaneously, significantly reducing the cost of dynamic dependency analysis. We evaluate MOAD by instantiating program slices from the obtained probabilistic dependency model. Compared to ORBS, MOAD's model construction requires only 18.7% of the observations used by ORBS, while its slices are only 16% larger than the corresponding ORBS slice, on average
Binding MOAD (Mother Of All Databases)
Binding MOAD (Mother of All Databases) is the largest collection of high-quality, protein–ligand complexes available from the Protein Data Bank. At this time, Binding MOAD contains 5331 protein–ligand complexes comprised of 1780 unique protein families and 2630 unique ligands. We have searched the crystallography papers for all 5000+ structures and compiled binding data for 1375 (26%) of the protein–ligand complexes. The binding-affinity data ranges 13 orders of magnitude. This is the largest collection of binding data reported to date in the literature. We have also addressed the issue of redundancy in the data. To create a nonredundant dataset, one protein from each of the 1780 protein families was chosen as a representative. Representatives were chosen by tightest binding, best resolution, etc. For the 1780 “best” complexes that comprise the nonredundant version of Binding MOAD, 475 (27%) have binding data. This significant collection of protein–ligand complexes will be very useful in elucidating the biophysical patterns of molecular recognition and enzymatic regulation. The complexes with binding-affinity data will help in the development of improved scoring functions and structure-based drug discovery techniques. The dataset can be accessed at http://www.BindingMOAD.org . Proteins 2005. © 2005 Wiley-Liss, Inc.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/48691/1/20512_ftp.pd
DOA Estimation in Multipath Environment with 2-Element Synthetic ULA
We propose a cost-efficient direction-of-arrival (DOA) estimation method using only two antenna elements, where one element is fixed and the other element moves in a straight line. It is shown that a uniform linear array (ULA) with multiple elements can be synthesized by dividing the sample from one element by that from the other. A high-resolution multiple-signal classification (MUSIC) algorithm based on smoothing is then applied to accurately estimate the DOAs of coherent sources. Numerical results show that the proposed method achieves a comparable DOA resolution and mean-squared error performance at moderate SNR when compared with the MUSIC algorithm applied to a conventional ULA.2
Digitalització i exhibició de l'exposició "Viaje a la Ciudad del Infinito" de la fundació Vicente Ferrer a través de la plataforma web MOAD
[CA] El treball desenvolupat en aquest TFG descriu tot el procés dut a terme per a traslladar
l’exposició Viaje a la Ciudad del Infinito, de la Fundació Vicente Ferrer al Museu Online
d’Art Digital (MOAD), una plataforma web dedicada a l’exposició de diferents obres
d’art.
El treball a desenvolupar s’estructura en dos parts, una primera part més teórica on
s’analitzen les necessitats de l’exposició respecte al disseny actual de MOAD, i una
segona part, on es presenta una proposta de disseny web per a l’exposició en MOAD
així com la implementació en llenguatges web.[EN] The work developed in this TFG describes the whole process carried out to move the exhibition Viaje a la Ciudad del Infinito, from the Vicente Ferrer Foundation to the Online Museum of Digital Art (MOAD), a web platform dedicated to the exhibition of different works of art.The work to be developed is structured in two parts, a first more theoretical part where the needs of the exhibition are analyzed with respect to the current design of MOAD, and a second part, where a web design proposal for the exhibition in MOAD as well as implementation in web languages.Vila Ridaura, M. (2021). Digitalització i exhibició de l'exposició "Viaje a la Ciudad del Infinito" de la fundació Vicente Ferrer a través de la plataforma web MOAD. Universitat Politècnica de València. https://riunet.upv.es/handle/10251/175638TFG
MOAD in the Classroom 2016-17 Evaluation Findings Report
MoAD in the Classroom (MIC) is an arts-based visual literacy and cultural studies program for third graders in the San Francisco Bay Area. Participating classes received two instructional visits to their classrooms by MIC instructors who introduced visual arts vocabulary, museum themes, and the current museum exhibitions. Classrooms also made two trips to the museum, during which they saw the exhibitions that they talked about in class, learned how to view and talk about art, and participated in hands-on art activities
UPDATING BINDING MOAD — DATA MANAGEMENT AND INFORMATION WORKFLOW
Binding MOAD (Mother of All Databases) is the largest collection of high-quality, protein-ligand complexes available from the Protein Data Bank. It has grown to 9837 hand-curated entries. Here, we describe our semi-annual updating procedures and BUDA (Binding Unstructured Data Analysis), a custom workflow tool that incorporates natural language processing technologies to facilitate the annotation process.Protein-ligand binding, database, natural language processing
IscS Functions as a Primary Sulfur-donating Enzyme by Interacting Specifically with MoeB and MoaD in the Biosynthesis of Molybdopterin inEscherichia coli
The persulfide sulfur formed on an active site cysteine residue of pyridoxal 5'-phosphate-dependent cysteine desulfurases is subsequently incorporated into the biosynthetic pathways of a variety of sulfur-containing cofactors and thionucleosides. In molybdenum cofactor biosynthesis, MoeB activates the C terminus of the MoaD subunit of molybdopterin (MPT) synthase to form MoaD-adenylate, which is subsequently converted to a thiocarboxylate for the generation of the dithiolene group of MPT. It has been shown that three cysteine desulfurases (CsdA, SufS, and IscS) of Escherichia coli can transfer sulfur from L-cysteine to the thiocarboxylate of MoaD in vitro. Here, we demonstrate by surface plasmon resonance analyses that IscS, but not CsdA or SufS, interacts with MoeB and MoaD. MoeB and MoaD can stimulate the IscS activity up to 1.6-fold. Analysis of the sulfuration level of MoaD isolated from strains defective in cysteine desulfurases shows a largely decreased sulfuration level of the protein in an iscS deletion strain but not in a csdA/sufS deletion strain. We also show that another iscS deletion strain of E. coli accumulates compound Z, a direct oxidation product of the immediate precursor of MPT, to the same extent as an MPT synthase-deficient strain. In contrast, analysis of the content of compound Z in Delta csdA and Delta sufS strains revealed no such accumulation. These findings indicate that IscS is the primary physiological sulfur-donating enzyme for the generation of the thiocarboxylate of MPT synthase in MPT biosynthesis
Binding MOAD (Mother of All Databases).
Binding MOAD (Mother of All Databases) is the largest collection of high-quality,
protein-ligand complexes available from the Protein Data Bank. Mining Binding MOAD
has revealed physical differences in how enzymes and nonenzymes bind small molecules.
High-affinity ligands of enzymes are much larger than those with low affinity, but highand
low-affinity ligands of nonenzymes are the same size. Furthermore, nonenzymes were found
to have higher ligand efficiencies. The different efficiencies are not due to differences in
the physicochemical properties of the ligands; instead, the amino-acid composition of the
pockets are very different despite very similar distributions of amino acids in the overall
protein sequences.
This study aims to address the issue of protein flexibility upon ligand binding. The
influence of ligand binding on protein flexibility is examined by analyzing a large number
of proteins crystallized with and without ligands. It is shown that, in general, ligand binding
stabilizes the protein and results in a smaller backbone root mean square deviation (RMSD)
among holo-protein structures, compared the backbone RMSD of the apo-protein structures.
Furthermore, the holo structures appear to sample a smaller subset of the space inhabited
by apo structures, because the difference between apo and holo structures is smaller than
variation seen among apo structures themselves. The size of the bound ligand does not
appear to matter in determining the rigidification. While ligand binding generally does
not induce large changes in the backbone, they are significant. Ligand binding does have
distinct impact on the active site, as revealed by all-atom, active-site RMSD and the range
of c1 variation. Greater variation has been found between these two groups as
opposed to within either group by themselves. This suggests that ligand binding induces
active-site side chains to occupy a different conformational space before and after binding.
The influence on the active site could not be easily attributed to features such as ligand size,
resolution, protein function, or catalytic composition.PhDBioinformaticsUniversity of Michigan, Horace H. Rackham School of Graduate Studieshttp://deepblue.lib.umich.edu/bitstream/2027.42/62331/1/mbensonz_1.pd
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