ModestR: a software tool for managing and analyzing species distribution map databases

The ModestR package consists of three applications: MapMaker, DataManager and MRFinder. MapMaker facilitates making range maps by drawing the areas, by importing existing data or using the Global Biodiversity Information Facility portal. It can discriminate between different habitats, thereby making data cleaning tasks easier. DataManager allows the management of taxonomically structured databases for range maps. MRFinder supports querying ModestR databases to find the species present in specific areas. Possible applications include the compilation and management of species distribution databases, cleaning data and computing aggregated data to perform subsequent analyses in other packages thanks to emphasized interoperability.     

0j.py: a software tool for low complexity proteins and protein domains

Low complexity proteins and protein domains have sequences which appear highly non-random. Over the years, these sequences have been routinely filtered out during sequence similarity searches because interest has been focused on globular proteins, and inclusion of these domains can severely skew search results. However, early work on these proteins and more recent studies of the related area of repeated protein sequences suggests that low complexity protein domains have function and therefore are in need of further investigation. 0j.py is a new tool for demarcating low complexity protein domains more accurately than has been possible to date. The paper describes 0j.py and its use in revealing proteins with repeated and poly-amino-acid peptides. Statistical methods are then employed to to examine the distribution of these proteins across species, while keyword clustering is used to suggest roles performed by proteins through the use of low complexity domains.     

Methods for analyzing peptides and proteins on a chromatographic timescale by electron-transfer dissociation mass spectrometry

Advancement in proteomics research relies on the development of new, innovative tools for identifying and characterizing proteins. Here, we describe a protocol for analyzing peptides and proteins on a chromatographic timescale by coupling nanoflow reverse-phase (RP) liquid chromatography (LC) to electron-transfer dissociation (ETD) mass spectrometry. For this protocol, proteins can be proteolytically digested before ETD analysis, although digestion is not necessary for all applications. Proteins 相似文献   

SCOPExplorer: a tool for browsing and analyzing structural classification of proteins (SCOP) data

We have developed a tool, named "SCOPExplorer", for browsing and analyzing SCOP information. SCOPExplorer 1) contains a tree-style viewer to display an overview of protein structure data, 2) is able to employ a variety of options to analyze SCOP data statistically, and 3) provides a function to link protein domains to protein data bank (PDB) resources. SCOPExplorer uses an XML-based structural document format, named "SCOPML", derived from the SCOP data. To evaluate SCOPExplorer, proteins containing more than 20 domains were analyzed. The Skp1-Skp2 protein complex and the Fab fragment of IgG2 contain the largest numbers of domains in the current eukaryotic SCOP database. These proteins are known to either bind to various proteins or generate diversity. This suggests that the more domains a protein has, the more interactions or more variability it will be capable of. (SCOPExplorer is available for download at http://scopexplorer.ulsan.ac.kr).     

Albumin immobilized on agarose as a tool for measuring ligand binding of proteins or peptides.

Bovine serum albumin immobilized on agarose has been tested in competitive binding studies as a means of measuring the binding of cortisol, tryptophan, fatty acids, and bilirubin to a number of albumins and albumin fragments. Chemical coupling of albumin to agarose does not appear to alter the primary binding sites for most ligands and the degree of ligand binding by immobilized albumin is comparable to that by soluble albumin. Evaluation of ligand binding by a protein based on its competition with immobilized protein is suggested as a convenient procedure particularly well suited to proteins and ligands whose size precludes investigation by dialysis or whose instability demands a rapid procedure.     

In vitro selection as a powerful tool for the applied evolution of proteins and peptides

New in vitro methods for the applied evolution of protein structure and function complement conventional cellular and phage-based methods. Strategies employing the direct physical linkage of genotype and phenotype, and the compartmental association of gene and product to select desired properties are discussed, and recent useful applications are described. Engineering of antibodies and other proteins, selection from cDNA libraries, and the creation of functional protein domains from completely random starting sequences illustrate the value of the in vitro approaches. Also discussed is an emerging new direction for in vitro display technology: the self-assembly of protein arrays.     

pkDACLASS: Open source software for analyzing MALDI-TOF data

In recent years, mass spectrometry has become one of the core technologies for high throughput proteomic profiling in biomedical research. However, reproducibility of the results using this technology was in question. It has been realized that sophisticated automatic signal processing algorithms using advanced statistical procedures are needed to analyze high resolution and high dimensional proteomic data, e.g., Matrix-Assisted Laser Desorption/Ionization Time-of-Flight (MALDI-TOF) data. In this paper we present a software package-pkDACLASS based on R which provides a complete data analysis solution for users of MALDITOF raw data. Complete data analysis comprises data preprocessing, monoisotopic peak detection through statistical model fitting and testing, alignment of the monoisotopic peaks for multiple samples and classification of the normal and diseased samples through the detected peaks. The software provides flexibility to the users to accomplish the complete and integrated analysis in one step or conduct analysis as a flexible platform and reveal the results at each and every step of the analysis. AVAILABILITY: The database is available for free at http://cran.r-project.org/web/packages/pkDACLASS/index.html.     

Ordination as a tool for analyzing complex data sets

Summary Ordination has proven to be a useful tool for examining relationships between environment and vegetation in data sets with a simple underlying environmental strueture. Complex data sets have proven much less tractable. A strategy is offered for dealing with complex data sets based on progressive removal of sets of stands along identified gradients, and subsequent reordination. This strategy is demonstrated using forests of the North Carolina piedmont.The author gratefully acknowledges the continuing collaboration of Dr. Norman L. Christensen of Duke University. This research was supported by National Science Foundation grants DEB-7708743 and DEB-7804043 to R.K.P. and DEB-7707532 and DEB-7804041 to N.L.C.     

BCETM: a tool for software integration

The integration of software into special-purpose systems (e.g.for gene sequence analysis) can be a difficult task. We describea general-purpose software integration tool, the BCETM program,that facilitates assembly of VAX-based software into applicationsystems and provides an easy-to-use, intuitive user interface.We describe the use of BCE to integrate a heterogeneous collectionof sequence analysis tools. Many BCE design features are generallyapplicable and can be implemented in other language or hardwareenvironments. Received on May 13, 1987; accepted on October 2, 1987     

BiVisu: software tool for bicluster detection and visualization

BiVisu is an open-source software tool for detecting and visualizing biclusters embedded in a gene expression matrix. Through the use of appropriate coherence relations, BiVisu can detect constant, constant-row, constant-column, additive-related as well as multiplicative-related biclusters. The biclustering results are then visualized under a 2D setting for easy inspection. In particular, parallel coordinate (PC) plots for each bicluster are displayed, from which objective and subjective cluster quality evaluation can be performed. Availability: BiVisu has been developed in Matlab and is available at http://www.eie.polyu.edu.hk/~nflaw/Biclustering/.     

MassSorter: a tool for administrating and analyzing data from mass spectrometry experiments on proteins with known amino acid sequences

Background  

Proteomics is the study of the proteome, and is critical to the understanding of cellular processes. Two central and related tasks of proteomics are protein identification and protein characterization. Many small laboratories are interested in the characterization of a small number of proteins, e.g., how posttranslational modifications change under different conditions.     

Self-assembling peptides and proteins for nanotechnological applications

Photolithography enables the precise construction of nanodevices in two-dimensional formats. However, self-assembly of designed molecules serves as an alternative for the construction of three-dimensional nanoscale systems and is particularly appealing in that material properties can potentially be engineered at the molecular level. Peptides and proteins hold promise as building blocks for self-assembled systems because of their exquisite three-dimensional structures and evolutionarily fine-tuned functions.     

Element-coded affinity tags for peptides and proteins

Isotope-coded affinity tags (ICAT) represent an important new tool for the analysis of complex mixtures of proteins in living systems [Aebersold, R., and Mann, M. (2003) Nature, 422, 198-207]. We envisage an alternative protein-labeling technique based on tagging with different element-coded metal chelates, which affords affinity chromatography, quantification, and identification of a tagged peptide from a complex mixture. As proof of concept, a synthetic peptide was modified at a cysteine side chain with either a carboxymethyl group or acetamidobenzyl-1,4,7,10-tetraazacyclododecane-N,N',N' ',N' "-tetraacetic acid (AcBD) chelates of terbium or yttrium. A mixture of the three modified peptides in a mole ratio of 100:1.0:0.83 carboxymethyl:AcBD-Tb:AcBD-Y was trypsinized, purified on a new affinity column that binds rare-earth DOTA chelates, and analyzed by LC-MS/MS. Chelate-tagged tryptic peptides eluted cleanly from the affinity column; the tagged peptides chromatographically coeluted during LC-MS analysis, were present in the expected ratio as indicated by MS ion intensity, and were sequence-identified by tandem mass spectrometry. DOTA-rare earth chelates have exceptional properties for use as affinity tags. They are highly polar and water-soluble. Many of the rare earth elements are naturally monoisotopic, providing a variety of simple choices for preparing mass tags. Further, the rare earths are heavy elements, whose mass defects give the masses of tagged peptides exact values not normally shared by molecules that contain only light elements.     

PhyloNet: a software package for analyzing and reconstructing reticulate evolutionary relationships

Background  

Phylogenies, i.e., the evolutionary histories of groups of taxa, play a major role in representing the interrelationships among biological entities. Many software tools for reconstructing and evaluating such phylogenies have been proposed, almost all of which assume the underlying evolutionary history to be a tree. While trees give a satisfactory first-order approximation for many families of organisms, other families exhibit evolutionary mechanisms that cannot be represented by trees. Processes such as horizontal gene transfer (HGT), hybrid speciation, and interspecific recombination, collectively referred to as reticulate evolutionary events, result in networks, rather than trees, of relationships. Various software tools have been recently developed to analyze reticulate evolutionary relationships, which include SplitsTree4, LatTrans, EEEP, HorizStory, and T-REX.     

Biana: a software framework for compiling biological interactions and analyzing networks

Background  

The analysis and usage of biological data is hindered by the spread of information across multiple repositories and the difficulties posed by different nomenclature systems and storage formats. In particular, there is an important need for data unification in the study and use of protein-protein interactions. Without good integration strategies, it is difficult to analyze the whole set of available data and its properties.     

Fluorescently labeled ribosomes as a tool for analyzing antibiotic binding

Measuring the binding of antibiotics and other small-molecular-weight ligands to the 2.5 MDa ribosome often presents formidable challenges. Here, we describe a general method for studying binding of ligands to ribosomes that carry a site-specific fluorescent label covalently attached to one of the ribosomal proteins. As a proof of principle, an environment-sensitive fluorescent group was placed at several specific sites within the ribosomal protein S12. Small ribosomal subunits were reconstituted from native 16S rRNA, individually purified small subunit proteins, and fluorescently labeled S12. The fluorescence characteristics of the reconstituted subunits were affected by several antibiotics, including streptomycin and neomycin, which bind in the vicinity of protein S12. The equilibrium dissociation constants of the drugs obtained using a conventional fluorometer were in good agreement with those observed using previously published methods and with measurements based on the use of radiolabeled streptomycin. The newly developed method is rapid and sensitive, and can be used for determining thermodynamic and kinetic binding characteristics of antibiotics and other small ribosomal ligands. The method can readily be adapted for use in high-throughput screening assays.