G. Sowmiya

Bioinformatics Institute of India, Noida, Uttar Pradesh, India

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Publications (7)16.02 Total impact

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    ABSTRACT: Small RNAs (sRNAs) are non-coding transcripts exerting their functions in the cells directly. Identification of sRNAs is a difficult task due to the lack of clear sequence and structural biases. Most sRNAs are identified within genus specific intergenic regions in related genomes. However, several of these regions remain un-annotated due to lack of sequence homology and/or potent statistical identification tools. A computational engine has been built to search within the intergenic regions to identify and roughly annotate new putative sRNA regions in Enterobacteriaceae genomes. It utilizes experimentally known sRNA data and their flanking genes/KEGG Orthology (KO) numbers as templates to identify similar sRNA regions in related query genomes. The search engine not only has the capability to locate putative intergenic regions for specific sRNAs, but also has the potency to locate conserved, shuffled or deleted gene clusters in query genomes. Because it uses the KO terms for locating functionally important regions such as sRNAs, any further KO number assignment to additional genes will increase the sensitivity. The PsRNA server is used for the identification of putative sRNA regions through the information retrieved from the sRNA of interest. The computing engine is available online at http://bioserver1.physics.iisc.ernet.in/psrna/ and http://bicmku.in:8081/psrna/.
    Genomics Proteomics & Bioinformatics 06/2010; 8(2):127-34. DOI:10.1016/S1672-0229(10)60014-9
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    ABSTRACT: MIPS (metal interactions in protein structures) is a database of metals in the three-dimensional macromolecular structures available in the Protein Data Bank. Bound metal ions in proteins have both catalytic and structural functions. The proposed database serves as an open resource for the analysis and visualization of all metals and their interactions with macromolecular (protein and nucleic acid) structures. MIPS can be searched via a user-friendly interface, and the interactions between metals and protein molecules, and the geometric parameters, can be viewed in both textual and graphical format using the freely available graphics plug-in Jmol. MIPS is updated regularly, by means of programmed scripts to find metal-containing proteins from newly released protein structures. The database is useful for studying the properties of coordination between metals and protein molecules. It also helps to improve understanding of the relationship between macromolecular structure and function. This database is intended to serve the scientific community working in the areas of chemical and structural biology, and is freely available to all users, around the clock, at http://dicsoft2.physics.iisc.ernet.in/mips/.
    Journal of Applied Crystallography 02/2010; 43(1). DOI:10.1107/S002188980903982X · 3.95 Impact Factor
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    ABSTRACT: By exploiting the fast-growing Internet technology, the interactive computing server Water Analysis Package (WAP, version 2.0) has been updated with more flexible options to better understand the role of the water O atoms present in three-dimensional macromolecular (protein or nucleic acid) structures. The updated robust server facilitates the computation and visualization of water molecules from various hydration shells, interfacial water molecules and those water molecules that stabilize various secondary structural elements. It is also possible to detect the interactions of water molecules with various parts (polar atoms, nonpolar atoms, main-chain and side-chain atoms) of the protein molecule. Furthermore, a molecular graphics visualization program is interfaced to display the nature of the interactions of the water molecules. The Protein Data Bank archive interfaced with the server is updated every week; hence users get to analyse the latest structures. The computing server can be obtained from http://dicsoft2.physics.iisc.ernet.in/wap/.
    Journal of Applied Crystallography 10/2008; 41(5):952-954. DOI:10.1107/S0021889808022073 · 3.95 Impact Factor
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    ABSTRACT: Distant repeats in protein sequence play an important role in various aspects of protein analysis. A keen analysis of the distant repeats would enable to establish a firm relation of the repeats with respect to their function and three-dimensional structure during the evolutionary process. Further, it enlightens the diversity of duplication during the evolution. To this end, an algorithm has been developed to find all distant repeats in a protein sequence. The scores from Point Accepted Mutation (PAM) matrix has been deployed for the identification of amino acid substitutions while detecting the distant repeats. Due to the biological importance of distant repeats, the proposed algorithm will be of importance to structural biologists, molecular biologists, biochemists and researchers involved in phylogenetic and evolutionary studies.
    Bioinformation 02/2008; 3(1):28-32. DOI:10.6026/97320630003028 · 0.50 Impact Factor
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    ABSTRACT: A computing engine, the Protein Structure Analysis Package (PSAP), has been developed to calculate and display various hidden structural and functional features of three-dimensional protein structures. The proposed computing engine has several utilities to enable structural biologists to analyze three-dimensional protein molecules and provides an easy-to-use Web interface to compute and visualize the necessary features dynamically on the client machine. Users need to provide the Protein Data Bank (PDB) identification code or upload three-dimensional atomic coordinates from the client machine. For visualization, the free molecular graphics programs RasMol and Jmol are deployed in the computing engine. Furthermore, the computing engine is interfaced with an up-to-date local copy of the PDB. The atomic coordinates are updated every week and hence users can access all the structures available in the PDB. The computing engine is free and is accessible online at http://iris.physics.iisc.ernet.in/psap/.
    Journal of Applied Crystallography 08/2007; 40. DOI:10.1107/S0021889807021875/he5372sup1.pdf · 3.95 Impact Factor
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    ABSTRACT: Ion pairs contribute to several functions including the activity of catalytic triads, fusion of viral membranes, stability in thermophilic proteins and solvent-protein interactions. Furthermore, they have the ability to affect the stability of protein structures and are also a part of the forces that act to hold monomers together. This paper deals with the possible ion pair combinations and networks in 25% and 90% non-redundant protein chains. Different types of ion pairs present in various secondary structural elements are analysed. The ion pairs existing between different subunits of multisubunit protein structures are also computed and the results of various analyses are presented in detail. The protein structures used in the analysis are solved using X-ray crystallography, whose resolution is better than or equal to 1.5 A and R-factor better than or equal to 20%. This study can, therefore, be useful for analyses of many protein functions. It also provides insights into the better understanding of the architecture of protein structure.
    Journal of Biosciences 07/2007; 32(4):693-704. DOI:10.1007/s12038-007-0069-1 · 1.94 Impact Factor
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    ABSTRACT: The Ramachandran plot displays the main chain conformation angles (Phi and Psi) of the polypeptide chain of a protein molecule. The paper reports the updated version of the Ramachandran plot web server and has several improved options for displaying the conformation angles in various regions. In addition, options are provided to display the conformation angles in various secondary structural elements and regions within the user specified Phi and Psi values in the plot. The updated version is accessible at the following URL: http://dicsoft1.physics.iisc.ernet.in/rp/.
    Protein and Peptide Letters 02/2007; 14(7):669-71. DOI:10.2174/092986607781483912 · 1.74 Impact Factor