Walk in interview for guest faculty in Pondicherry University, India. For more information please visit http://www.bicpu.edu.in/bioinfor140814.pdf

Requirements

You are (or soon will be) a master in bio-informatics. You have strong ICT skills and you are eager to fully submerge into the world of protein modeling. You have good experience with Linux and one or more programming languages as well as knowledge of tertiary structure analysis. Candidates with a Master degree in one of the life sciences (Biomedical sciences, Biochemistry, Bio-engineering, Biostatistics, …), with relevant interest and extended experience in this field are also welcome. A general background cancer biology and genetics is needed. You are willing and eligible to apply for a personal PhD fellowship with the Flemish FWO (FWO.be). Therefore, it is required that you hold a master degree from a European university, and have not obtained your master diploma more than three years ago (see FWO website for detailed conditions). Proficiency in English, and good communication skills, both oral and written, are required. You are highly motivated, and you like to work in an interactive research team. You are willing to work on a 4-year PhD project starting beginning of 2020.

What we offer

We offer a one year position, as a PhD student, which can be extended up to 4 year upon positive evaluation, even if a personal fellowship application is not successful. Wages are according to the standard Flemish bursary levels for PhD students.

Interested?
For additional information please contact dr. Geert Vandeweyer. To apply, send a copy of your CV including details of your relevant skills and a motivation letter by e-mail to dr. Geert Vandeweyer (geert.vandeweyer@uantwerpen.be) before March 15, 2020.

Source:https://academicpositions.be/ad/university-of-antwerp/2020/phd-student-bio-informatician-in-computational-protein-modeling/141252?utm_source=jooble&utm_medium=cpc&utm_campaign=jooble

DNAApp: for iPhone/iPad

This is an iOS app that allows for the opening and analysis of DNA sequencing files - ab1. It includes handy tools such as "Reverse Complement", "Jump to", "Copy and Paste sequences", fast and end scrolling, "Chromatogram adjustments", and "Searching for segments" functions.
When used in combination with other zip apps, and also web-tools like Blast, this app allows you to analyze, and also determine the quality of your sequencing files.
This app works with cloud storage access like Dropbox to your sequencing files.
This is now compatible with the new update for iOS 7.1.
Demo video can be found at: https://www.youtube.com/watch?v=mXeo9hXdZgM 

More @ https://itunes.apple.com/us/app/dnaapp/id854944694?mt=8

DNAApp: For android

This is the first android app that allows for the opening and analysis of DNA sequencing files - ab1. It includes handy tools such as "Reverse Complement", "Jump to", fast and end scrolling, "Chromatogram adjustments", amino acid translations, "export to fasta", and "searching for segment" function.

• When used in combination with other zip apps, and also web-tools like Blast, this app allows you to analyze, and also determine the quality of your sequencing files.
• This app works with cloud storage access like Dropbox to your sequencing files.
• This is now compatible with the new update for Android 4.4.2.

More @  https://play.google.com/store/apps/details?id=bii.seqdatreader&hl=en

BioGene:iPhone/iPad

BioGene is an information tool for biological research. Use BioGene to learn about gene function. Enter a gene symbol or gene name, for example "CDK4" or "cyclin dependent kinase 4" and BioGene will retrieve its gene function and references into its function (GeneRIF).

• BioGene was produced in affiliation with the Computational Biology Center at Memorial Sloan-Kettering Cancer Center with primary information from Entrez Gene at the NCBI.

More @  https://itunes.apple.com/us/app/biogene/id333180084?mt=8

Mentha - the interactome browser: Android

About: mentha - the interactome browser, is a project that offers protein-protein physical/enzymatic interaction information from various sources. For more details about mentha, visit mentha's website. This client application is an independent project. This application is designed to allow you to search proteins on the go.

Key features (Also in website):

• Search proteins by UniProt IDs, gene name or keywords
• Collect proteins from different queries.
• Spot common interactors in clusters.
• Easily distinguish between proteins from Homo sapiens and other organisms (Yellow rounded rectangles)
• Click on edges(links) to get scientific evidence.
• Click on proteins to see descriptions.

More @  https://play.google.com/store/apps/details?id=com.sinnefa.mentha&hl=en

GeneIndex: iPhone/iPad

GeneIndex quickly provides information about genes from various sources. It also includes a RSS reader for journal feeds as well as a PubMed viewer.

Key Features:

• Look up genes by symbol or description.
• Gene indexes for many mammals, plants, invertebrates, and bacteria.
• Link to gene info on websites.
• Download files for offline use. (.pdf, .mp3, .m4v, .doc, .ppt, .xls )
• transfer files via open in, email, or iTunes file sharing
• View RSS feeds for journals
• Query GeneRIF interactions, COSMIC mutations, and CNV data for cell lines.
• Does not require a network connection for local databases.
• View and search PubMed in table view.

GeneIndex provides a convenient and portable way to lookup gene symbols while at a seminar, conference, or lab meeting. Genes are linked to common life science websites such as NCBI, COSMIC, KEGG, PubMed, SymAtlas, UCSC genome browser, Pathway Commons, Genatlas, Wikipedia, HUGO, and OMIM. GeneRIF gene interactions can also be queried.

• Keep current on the scientific literature. GeneIndex includes a RSS reader and web browser for browsing popular journals like Nature, Science, and Cell. You can also add your own RSS feeds. PDFs and podcasts can be saved as files that you can view on the device or email as attachments.
• Examine the status of genes in common cell lines. A subset of COSMIC containing cell lines can be queried for mutations. Copy Number Variation (CNV) plots from cell lines profiled by GSK and Sanger are also linked to genes.

More @  https://itunes.apple.com/us/app/geneindex/id319769866?mt=8

Genome Voyager: iPad

Gain first hand experience identifying the genomic basis of disease by analyzing cases with whole genome sequencing data that have been published for research and learning purposes.

• Visualize whole human genome sequencing data including small variations, copy number variations (CNVs), and loss of heterozygosity (LOH) events
• Quickly find variants of interest by filtering variants based on associated genes, functional impact, allele frequency in data sets, and cross-references with various genomic databases.
• Collaborate on variant assessments with other researchers and academics to improve knowledge of both pathogenic and benign variants.
  To use Genome Voyager, users must join Genome Voyager’s community of researchers and academics. Visit http://voyager.completegenomics.com to signup.

More @  https://itunes.apple.com/us/app/genome-voyager/id637353801?mt=8

YeastGenome: iPhone/iPad

Use YeastGenome to quickly find fundamental information about Saccharomyces cerevisae genes and chromosomal features. Search gene names, gene descriptions or browse the database to find information about your favorite gene, as well as more detailed information such as Gene Ontology, mutant phenotype, and protein and genetic interaction data.
YeastGenome contains the latest from the Saccharomyces Genome Database (www.yeastgenome.org) in an on bound app database. As more detailed information is presented the app switches to web services access to SGD, and then for even more details provides complete information via hyperlinks to the appropriate SGD database pages.

Key features:

• Search using gene name or keywords
• Browse by feature type
• Save your favorite features
• Can be used in airplane mode
• Email information about features to collaborators

What's New in Version 1.8.1

• This update is required to provide continued functionality. Some of the data provided by this app accesses the SGD service using a method that is changing in May 2013. This version provides changes to allow access to continue. The on board database of yeast gene information has also been updated to March 2013.

More @  https://itunes.apple.com/us/app/yeastgenome/id520868597?mt=8

SNPdbe: iPhone/iPad

SNPdbe — SNP database of effects, with predictions of computationally annotated functional impacts of SNPs. Database entries represent nsSNPs in dbSNP and 1000 Genomes collection, as well as variants from UniProt and PMD. SAASs come from >2600 organisms; ‘human’ being the most prevalent. The impact of each SAAS on protein function is predicted using the SNAP and SIFT algorithms and augmented with experimentally derived function/structure information and disease associations from PMD, OMIM and UniProt.

More @  https://itunes.apple.com/us/app/snpdbe/id588289719?mt=8

SimGene: iPhone/iPad / Android

SimGene: for iPhone/iPad

SimGene is an iPhone/iPad/iPod touch application designed for molecular biologists, bioinformaticians and medical researchers. The application interfaces with Simbiot, Ensembl, NCBI, Gene Ontology, KEGG Pathways, PubMed, Genomic Variations and many other databases to retrieve up-to-date annotation information for over 30 species, based on gene symbol search. The application provides gene and transcript cross reference information for NCBI, Ensembl, RefSeq and UniProt. SimGene also contains an integrated genome browser with information on genes, transcripts, exons and SNPs.

More @  https://itunes.apple.com/us/app/simgene/id427772349?mt=8

SimGene: for Android

bioinformaticians and medical researchers. The application interfaces with Simbiot,Ensembl, NCBI, Gene Ontology, KEGG Pathways, PubMed, Genomic Variations andmany other databases to retrieve up-to-date annotation information for over 30species, based on gene symbol search. The application provides gene and transcriptcross reference information for NCBI, Ensembl, RefSeq and UniProt. SimGene alsocontains an integrated genome browser with information on genes, transcripts,exons and SNPs.

More @  https://play.google.com/store/apps/details?

TimeTree: iPhone/iPad

TimeTree is a public knowledge-base for information on the evolutionary timescale of life. This application allows easy exploration of the thousands of divergence times among organisms in the scientific literature. A tree-based (hierarchical) system is used to identify all published molecular time estimates bearing on the divergence of two chosen organisms, such as species, compute summary statistics, and present the results. Names of two taxa to be compared are entered in the search window and the results are presented on a set of self-explanatory tabs.

• TimeTree 3.0 was released September 27, 2011 with new data from 1209 studies including 25342 time nodes. We will be adding more data in the future as it comes in from researchers.
• TimeTree is jointly directed by Blair Hedges (Pennsylvania State University) and Sudhir Kumar (Arizona State University). This project has been supported, in part, by grants from the National Science Foundation, National Institutes of Health, NASA Astrobiology Institute, and Science Foundation of Arizona.

More @  https://itunes.apple.com/us/app/timetree/id372842500?mt=8

GeneGroove: iPhone/iPad

GeneGroove is the first application to create a music melody from DTC-Genomics data. If you own 23andMe (Mountain View, CA) personal genomic results, GeneGroove will create for you a unique melody intimately based on your 23andMe genome informations. The music in you.

• After uploading your 23andMe raw data onto your iPhone via iTunes, GeneGroove will analyze your genome informations and generate a unique identifier key. This key, called the GeNumber, will embed the uniqueness of your genome data while keeping your privacy safe, and will be used by GeneGroove to generate your music melody.
• The GeNumber doesn't contain anymore genomic information but it is based on your genome and it is unique, it is yours. It will be used in upcoming Portable Genomics applications to mix and remix music, manipulate sounds and share your art with your friends and family.

More @  https://itunes.apple.com/us/app/genegroove/id492247404?mt=8

CASTp : http://sts.bioengr.uic.edu/castp/  Computed Atlas of Surface Topography of proteins (CASTp) provides an online resource for locating, delineating and measuring concave surface regions on three-dimensional structures of proteins. These include pockets located on protein surfaces and voids buried in the interior of proteins. The measurement includes the area and volume of pocket or void by solvent accessible surface model (Richards' surface) and by molecular surface model (Connolly's surface), all calculated analytically. CASTp can be used to study surface features and functional regions of proteins. CASTp includes a graphical user interface, flexible interactive visualization, as well as on-the-fly calculation for user uploaded structures. CASTp is updated daily and can be accessed at http://cast.engr.uic.edu.

LigASite: http://www.bigre.ulb.ac.be/Users/benoit/LigASite/index.php?home is a gold-standard dataset of biologically relevant binding sites in protein structures. It consists of proteins with one unbound structure and at least one structure of the protein-ligand complex. Both a redundant and a non-redundant (sequence identity lower than 25%) version is available. Quaternary structures proposed by PISA (3) are used for all structures in the dataset.

PDBeMotif: http://www.ebi.ac.uk/pdbe-site/pdbemotif/ is an extremely fast and powerful search tool that facilitates exploration of the Protein Data Bank (PDB) by combining protein sequence, chemical structure and 3D data in a single search. Currently it is the only tool that offers this kind of integration at this speed. PDBeMotif can be used to examine the characteristics of the binding sites of single proteins or classes of proteins such as Kinases and the conserved structural features of their immediate environments either within the same specie or across different species. For example, it can highlight a conserved activation loop common to protein kinases, which is important in regulating activity and is marked by conserved DFG and APE motifs at the start and end of the loop, respectively. The prediction of the effect of modifications to small molecules that bind to the active and/or regulatory sites of proteins on their efficacy can be based on the outcome of analytic work done using PDBeMotif.

fPOP: http://pocket.uchicago.edu/fpop/ (footprinting Pockets Of Proteins, http://pocket.uchicago.edu/fpop/) is a database of the protein functional surfaces identified by shape analysis. In this relational database, we collected the spatial patterns of protein binding sites including both holo and apo forms from more than 40,000 structures. To identify protein binding sites, we model the shape of a split pocket induced by a binding ligand(s). Essentially, we use a purely geometric method to extract site-specific spatial patterns of split pockets as templates to match those from unbound structures. To perform an effective shape comparison, we utilize the Smith-Waterman algorithm to footprint an unbound pocket fragment with those selected from the canonical functional surfaces of >19,000 structures in the SplitPocket (http://pocket.uchicago.edu/). The pairwise alignment of the unbound and split-pocket fragments is superimposed to evaluate the local structural similarity for detecting the unbound split characteristic through the RMSD measurement. Furthermore, we conduct a large-scale computation to systematically identify binding sites of proteins. In addition to the geometric measurements, we extensively measure the propensity of surface conservation encapsulated in the evolutionary history.(more)

metaPocket: http://metapocket.eml.org/  is a meta server to identify pockets on protein surface to predict ligand-binding sites. The identification of ligand-binding sites is often the starting point for protein function annotation and structure-based drug design. Many computational methods for the prediction of ligand-binding sites have been developed in recent decades. Here we present a consensus method metaPocket, in which the predicted sites from four methods: LIGSITE^cs, PASS, Q-SiteFinder, and SURFNET are combined together to improve the prediction success rate. All these methods are evaluated on two datasets of 48 unbound/bound structures and 210 bound structures. The comparison results show that metaPocket improves the success rate from 70 to 75% at the top 1 prediction. MetaPocket is available at http://metapocket.eml.org.

PocketQuery: http://pocketquery.csb.pitt.edu/  is a web service for interactively exploring not only hot spot and anchor residues, but hot regions, defined by clusters of residues, at the interface of protein-protein interactions. An assortment of metrics, including changes in solvent accessible surface area, energy-based scores, and sequence conservation, are available to screen and sort clusters of residues. PocketQuery was developed by David Koes from the Camacho Lab in the Department of Computational and System Biology at the University of Pittsburgh.

IBIS: http://www.ncbi.nlm.nih.gov/Structure/ibis/ibis.cgi is the NCBI Inferred Biomolecular Interactions Server. For a given protein sequence or structure query, IBIS reports physical interactions observed in experimentally-determined structures for this protein. IBIS also infers/predicts interacting partners and binding sites by homology, by inspecting the protein complexes formed by close homologs of a given query. To ensure biological relevance of inferred binding sites, the IBIS algorithm clusters binding sites formed by homologs based on binding site sequence and structure conservation.

3DLigandStie: http://www.sbg.bio.ic.ac.uk/~3dligandsite/ is an automated method for the prediction of ligand binding sites. Users can either submit a sequence or a protein structure. If a sequence is submitted then Phyre is run to predict the structure. The structure is then ussed to search a structural library to identify homologous structures with bound ligands. These ligands are superimposed onto the protein structure to predict a ligand binding site.

SitesBase: http://www.modelling.leeds.ac.uk/sb/ is a database of known ligand binding sites within the PDB which is navigable by PDB identifier or ligand 3 letter code e.g. NAD. Each binding site has a frequently updated register of structurally similar binding sites sharing atomic similarity detected by geometric hashing (Brakoulias and Jackson 2004). Multiple alignments, structural superpositions and links to other structural databases are also available enabling further analysis.

PROSURFER: http://163.43.140.95/top contains information about structural similarities with respect to the query surfaces. A pocket search algorithm detected 48,347 potential ligand binding sites from the 9,708 non-redundant protein entries in the PDB database. All-against-all structural comparison was performed for the predicted sites, and the similar sites with the Z-score ≥ 2.5 were selected. These results can be accessed by the PDB code or ligand name.

KBDOCK: http://kbdock.loria.fr/index.php is a 3D database system that defines and spatially clusters protein binding sites for knowledge-based protein docking. KBDOCK integrates protein domain-domain interaction information from 3DID and sequence alignments from PFAM together with structural information from the PDB in order to analyse the spatial arrangements of DDIs by Pfam family, and to propose structural templates for protein docking. [More]

Pocketome: http://www.pocketome.org/ The Pocketome is an encyclopedia of conformational ensembles of all druggable binding sites that can be identified experimentally from co-crystal structures in the Protein Data Bank.

sc-PDB: http://cheminfo.u-strasbg.fr:8080/scPDB/2011/db_search/about_scpdb.html  To assist structure-based approaches in drug design, we have processed the PDB to identify binding sites suitable for the docking of a drug-like ligand and we have so created a database called sc-PDB. The sc-PDB database provides separated MOL2 files for the ligand, its binding site and the corresponding protein chain(s). Ions and cofactors at the vicinity of the ligand are included in the protein. More details about the sc-PDB scope, its content and its evolution during the 2004-2009 period are provided in a pdf document.

The FunFOLD Binding Site Residue Prediction Server: BACKGROUND: The accurate prediction of ligand binding residues from amino acid sequences is important for the automated functional annotation of novel proteins. In the previous two CASP experiments, the most successful methods in the function prediction category were those which used structural superpositions of 3D models and related templates with bound ligands in order to identify putative contacting residues. However, whilst most of this prediction process can be automated, visual inspection and manual adjustments of parameters, such as the distance thresholds used for each target, have often been required to prevent over prediction. Here we describe a novel method FunFOLD, which uses an automatic approach for cluster identification and residue selection. The software provided can easily be integrated into existing fold recognition servers, requiring only a 3D model and list of templates as inputs. A simple web interface is also provided allowing access to non-expert users. The method has been benchmarked against the top servers and manual prediction groups tested at both CASP8 and CASP9.RESULTS: The FunFOLD method shows a significant improvement over the best available servers and is shown to be competitive with the top manual prediction groups that were tested at CASP8. The FunFOLD method is also competitive with both the top server and manual methods tested at CASP9. When tested using common subsets of targets, the predictions from FunFOLD are shown to achieve a significantly higher mean Matthews Correlation Coefficient (MCC) scores and Binding-site Distance Test (BDT) scores than all server methods that were tested at CASP8. Testing on the CASP9 set showed no statistically significant separation in performance between FunFOLD and the other top server groups tested. CONCLUSIONS: The FunFOLD software is freely available as both a standalone package and a prediction server, providing competitive ligand binding site residue predictions for expert and non-expert users alike. The software provides a new fully automated approach for structure based function prediction using 3D models of proteins.

ProBiS: http://probis.cmm.ki.si/index.php  algorithm for detection of structurally similar protein binding sites by local structural alignment. Motivation: Exploitation of locally similar 3D patterns of physicochemical properties on the surface of a protein for detection of binding sites that may lack sequence and global structural conservation. Results: An algorithm, ProBiS is described that detects structurally similar sites on protein surfaces by local surface structure alignment. It compares the query protein to members of a database of protein 3D structures and detects with sub-residue precision, structurally similar sites as patterns of physicochemical properties on the protein surface. Using an efficient maximum clique algorithm, the program identifies proteins that share local structural similarities with the query protein and generates structure-based alignments of these proteins with the query. Structural similarity scores are calculated for the query protein's surface residues, and are expressed as different colors on the query protein surface. The algorithm has been used successfully for the detection of protein–protein, protein–small ligand and protein–DNA binding sites. Availability: The software is available, as a web tool, free of charge for academic users at http://probis.cmm.ki.si

Active Site prediction: http://www.scfbio-iitd.res.in/dock/ActiveSite_new.jsp Active Site Prediction of Protein server computes the cavities in a given protein.

DEPTH: http://mspc.bii.a-star.edu.sg/tankp/run_depth.html Depth measures the closest distance of a residue/atom to bulk solvent. Accessible surface area is a parameter that is widely used in analyses of protein structure and stability. However accessible surface area does not distinguish between atoms just below the protein surface and those in the core of the protein. In order to differentiate between such buried residues, we describe a computational procedure for calculating the depth of a residue from the protein surface. A detailed description of the computation of depth can be found here.

FINDSITE: http://cssb.biology.gatech.edu/findsite  FINDSITE is a threading-based binding site prediction/protein functional inference/ligand screening algorithm that detects common ligand binding sites in a set of evolutionarily related proteins. Crystal structures as well as protein models can be used as the target structures.

PocketDepth: http://proline.physics.iisc.ernet.in/pocketdepth/  A new depth based algortihm for identification of ligand binding sites. Abstract: Computational methods for identifying and predicting functional sites in protein structures are increasingly becoming important in structural biology and bioinformatics not only for understanding the function of the molecule in detail but also for structure-based design of possible ligands and potential drugs as well as modified protein molecules. While there are a few structure based prediction methods already available, given the complexity and diversity of protein structural types, there is still a great need to explore newer methods and concepts to develop accurate, versatile and efficient binding site prediction algorithms. We have developed a new method PocketDepth, for identification of binding sites in proteins. The method is purely geometry-based and proceeds in two stages, labeling of grid cells with depth factors followed by a depth based clustering that uses neighbourhood information. Depth is an important parameter considered during protein structure visualization and analysis but has been used more often intuitively than systematically. Our current implementation of depth reflects how central a given sub-space is to a putative pocket rather than reflecting merely how far away it is situated from the nearest external surface of the protein. We have tested the algorithm against PDBbind, a large curated set of 1091 proteins obtained from PDB. A prediction was considered a true-positive if the predicted pocket had at-least 10% overlap with the actual ligand. The prediction accuracy using this set was about 96%. Moreover, 87% of the true-positives were identified within the first five ranks for each protein, of which 55% are in the first rank itself. 77% of the predictions had at least 50% overlap with the experimentally observed ligand. High prediction rates were again observed, when the method was tested against a data-set of apo-proteins and compared with their respective ligand complexes. A comparison of our method with four other widely used methods for a chosen representative set is also presented.

GHECOM 1.0 : http://strcomp.protein.osaka-u.ac.jp/ghecom/  Grid-based HECOMi finder. A program for finding multi-scale pockets on protein surfaces using mathematical morphology

Pocket-Finder: http://www.modelling.leeds.ac.uk/pocketfinder/ is based on the Ligsite algorithm written by Hendlich et al. (1997). Pocket-Finder was written to compare pocket detection with our new ligand binding site detction algorithm Q-SiteFinder.

Screen2: http://luna.bioc.columbia.edu/honiglab/screen2/cgi-bin/screen2.cgi  is a tool for identifying protein cavities and computing cavity attributes that can be applied for classification and analysis. The original Screen, written by Murad Nayal, was dependent on the obsolete Irix platform and is no longer available. Screen2 was reengineered by Brian Y. Chen for efficiency and compatibility, and made accessible as a web service by Raquel Norel.

ConCavity: http://compbio.cs.princeton.edu/concavity/ Identifying a protein's functional sites is an important step towards characterizing its molecular function. Numerous structure- and sequence-based methods have been developed for this problem. Here we introduce ConCavity, a small molecule binding site prediction algorithm that integrates evolutionary sequence conservation estimates with structure-based methods for identifying protein surface cavities. In large-scale testing on a diverse set of single- and multi-chain protein structures, we show that ConCavity substantially outperforms existing methods for identifying both 3D ligand binding pockets and individual ligand binding residues. As part of our testing, we perform one of the first direct comparisons of conservation-based and structure-based methods. We find that the two approaches provide largely complementary information, which can be combined to improve upon either approach alone. We also demonstrate that ConCavity has state-of-the-art performance in predicting catalytic sites and drug binding pockets. Overall, the algorithms and analysis presented here significantly improve our ability to identify ligand binding sites and further advance our understanding of the relationship between evolutionary sequence conservation and structural and functional attributes of proteins. Data, source code, and prediction visualizations are available on the ConCavity web site (http://compbio.cs.princeton.edu/concavit​y/).

MultiBind and MAPPIS: http://bioinfo3d.cs.tau.ac.il/MultiBind/index.html Web servers for multiple alignment of protein 3D binding sites and their interactions. Analysis of protein–ligand complexes and recognition of spatially conserved physico-chemical properties is important for the prediction of binding and function. Here, we present two webservers for multiple alignment and recognition of binding patterns shared by a set of protein structures. The first webserver, MultiBind (http://bioinfo3d.cs.tau.ac.il/MultiBind), performs multiple alignment of protein binding sites. It recognizes the common spatial chemical binding patterns even in the absence of similarity of the sequences or the folds of the compared proteins. The input to the MultiBind server is a set of protein-binding sites defined by interactions with small molecules. The output is a detailed list of the shared physico-chemical binding site properties. The second webserver, MAPPIS (http://bioinfo3d.cs.tau.ac.il/MAPPIS), aims to analyze protein–protein interactions. It performs multiple alignment of protein–protein interfaces (PPIs), which are regions of interaction between two protein molecules. MAPPIS recognizes the spatially conserved physico-chemical interactions, which often involve energetically important hot-spot residues that are crucial for protein–protein associations. The input to the MAPPIS server is a set of protein-protein complexes. The output is a detailed list of the shared interaction properties of the interfaces.

MolAxis: http://bioinfo3d.cs.tau.ac.il/MolAxis/  is a tool for the identification of high clearance pathways or corridors which represent molecular channels in the complement space of proteins. It is extremely efficient because it samples the medial axis of the complement of the molecule, reducing the problem dimension to two, since the medial axis is composed of surface patches. It is designed to analyze proteins channels, calculate pore dimensions and analyze atom accessibility. MolAxis reads files in the standard Protein Data Bank format (PDB) containing a single frame or multiple frames generated by molecular dynamics (MD) simulations. MolAxis handles two distinct scenarios: It computes channels that connect a single point (like an inner chamber) to the bulk solvent, and it also computes transmembrane (TM) channels. MolAxis has a friendly web interface (see the Web Server tab). It also has a stand-alone version, statically compiled for linux, which can be downloaded from the Download tab.

fpocket: http://fpocket.sourceforge.net/ fpocket is a very fast open source protein pocket (cavity) detection algorithm based on Voronoi tessellation. It was developed in the C programming language and is currently available as command line driven program. A GUI is in development and mdpocket (fpocket on md trajectories) is out now. fpocket includes two other programs (dpocket & tpocket) that allow you to extract pocket descriptors and test own scoring functions respectively. Furthermore a nifty druggability prediction score has been added to fpocket recently. As the algorithm is very fast it can be used on a large scale level (PDB size for instance). If you use fpocket for publication, please cite : Vincent Le Guilloux, Peter Schmidtke and Pierre Tuffery, "Fpocket: An open source platform for ligand pocket detection", BMC Bioinformatics, 2009, 10:168

SuMo: http://sumo-pbil.ibcp.fr/cgi-bin/sumo-welcome allows you to screen the Protein Data Bank (PDB) for finding ligand binding sites matching your protein structure or inversely, for finding protein structures matching a given site in your protein. This method is neither based on aminoacid sequence nor on fold comparisons. Priority is given to biological relevance. SuMo uses its own heuristics for defining ligand binding sites. Automatically selected ligand binding sites are extracted from PDB structure files and stored into SuMo's own database.

CAVER: http://www.caver.cz/ CAVER is a software tool for analysis and visualization of tunnels and channels in protein structures. Tunnels are void pathways leading from a cavity buried in a protein core to the surrounding solvent. Unlike tunnels, channels lead through the protein structure and their both endings are opened to the surrounding solvent. Studying of these pathways is highly important for drug design and molecular enzymology.

SiteHound: http://scbx.mssm.edu/sitehound/sitehound-download/download.html SiteHound identifies protein regions that are likely to interact with ligands. The only input files required by SITEHOUND are the PDB file of the protein and the Molecular Interaction Field (MIFs) or Affinity Map for that protein structure structure. EasyMIFs is provided as a tool to calculate MIFs, alternatively AutoGrid (part of the AutoDock suite developed by Arthur Olson’s group at The Scripps Research Insitute) or the SiteHound-web server can be used to produce Affinity maps or MIFs. A python script named 'auto.py' is provided in the package and can be used to perform binding site identification in a fully automated fashion. The script will prepare the protein PDB file, compute a Molecular Interaction Fields map with EasyMIFs and carry out binding site identification using SiteHound. It is also possible to use EasyMIFs and SiteHound separately.

SURFNET: http://www.biochem.ucl.ac.uk/~roman/surfnet/surfnet.html The SURFNET program generates surfaces and void regions between surfaces from coordinate data supplied in a PDB file.

MSPocket: http://appserver.biotec.tu-dresden.de/MSPocket/ is an orientation independent program for the detection and graphical analysis of protein surface pockets [Zhu2011]. The approach is based on the solvent excluded surfaces generated by MSMS [Sanner1996].

Pfinder : http://pdbfun.uniroma2.it/pfinder/index.html  Pfinder is a bioinformatic method for the prediction of phosphate-binding sites in protein structures. Given a protein structure, Pfinder compares it with a set of 215 highly conserved structural motifs known to bind the phosphate moiety of phosphorylated ligands.

VOIDOO: http://xray.bmc.uu.se/usf/voidoo.html is a program for detection of cavities in macromolecular structures. It uses an algorithm that makes it possible to detect even certain types of cavities that are connected to "the outside world". Three different types of cavity can be handled by VOIDOO: Vanderwaals cavities (the complement of the molecular Vanderwaals surface), probe-accessible cavities (the cavity volume that can be occupied by the centres of probe atoms) and MS-like probe-occupied cavities (the volume that can be occupied by probe atoms, i.e. including their radii).

PocketPicker: http://gecco.org.chemie.uni-frankfurt.de/pocketpicker/index.html Background: Identification and evaluation of surface binding-pockets and occluded cavities are initial steps in protein structure-based drug design. Characterizing the active site's shape as well as the distribution of surrounding residues plays an important role for a variety of applications such as automated ligand docking or in situ modeling. Comparing the shape similarity of binding site geometries of related proteins provides further insights into the mechanisms of ligand binding. Results: We present PocketPicker, an automated grid-based technique for the prediction of protein binding pockets that specifies the shape of a potential binding-site with regard to its buriedness. The method was applied to a representative set of protein-ligand complexes and their corresponding apo-protein structures to evaluate the quality of binding-site predictions. The performance of the pocket detection routine was compared to results achieved with the existing methods CAST, LIGSITE, LIGSITE^cs, PASS and SURFNET. Success rates PocketPicker were comparable to those of LIGSITE^cs and outperformed the other tools. We introduce a descriptor that translates the arrangement of grid points delineating a detected binding-site into a correlation vector. We show that this shape descriptor is suited for comparative analyses of similar binding-site geometry by examining induced-fit phenomena in aldose reductase. This new method uses information derived from calculations of the buriedness of potential binding-sites. Conclusion: The pocket prediction routine of PocketPicker is a useful tool for identification of potential protein binding-pockets. It produces a convenient representation of binding-site shapes including an intuitive description of their accessibility. The shape-descriptor for automated classification of binding-site geometries can be used as an additional tool complementing elaborate manual inspections.

McVol: http://www.bisb.uni-bayreuth.de/index.php?page=data/mcvol/mcvol  This program was developed to integrate the molecular volume, solven accessible volume an Van der Waals volume of proteins using a Monte carlo algorithm. Based on this calculations, McVol is also able to identify internal cavities as well as surface clefts und fill these cavities with water molecules. Additionally, a membrane of dummy atoms can be placed as a disc atound the protein. The program is available under the Gnu Public Licence. A precompiled binary (X86) can be downloaded free of charge from here (when the associated paper is published).

Our present objectives is to identify and isolate the substances secreted by Spalax cells, resolve with which components they interact that are active only on cancer cells, in order to unravel the biological mechanisms and pathways that evolved in Spalax cell machinery and ultimately lead to the death of cancer-cells. The study could attest to be a breakthrough in cancer research, using the long lived, hypoxia- and cancer-tolerant Spalax as a significant biological resource for biomedical research that hopefully could open new horizons in treatment and prevention of cancer in humans.

Contact: The applications should be submitted, together with extended CV and bibliography, summary of past accomplishments, and contact information of 3 referees, to Prof of Research Aaron Avivi (aaron@research.haifa.ac.il) AND Dr. Imad Shams (imadshams@gmail.com). (http://bit.ly/1lywShk) aaron@research.haifa.ac.il

More at http://evolution.haifa.ac.il/index.php/29-people/personal-websites/77-personal-site-avivi

Address of the bookmark: http://www.compbio.dundee.ac.uk/jpred4/

The Role

We are looking for a Software Engineer - Computational Biologist with 3+
years' experience in a similar role to design and implement a backend system
to support an online individualised genomics interface. This position is a
great opportunity for an ambitious, self-motivated individual to work in a
demanding, challenging and interesting role.

Position Description:
. Participate in planning, design, and implementation of Equinome back
end systems and technologies.
. Implement interfaces and management tools for back end services.
. Manage, analyse, interpret and visualise large genomics data sets.
. Work closely with scientific team to develop new features and
application enhancements
. Design, develop and manage a genomics research database.

Qualification/Experience:
. Minimum MSc in Computer Science, Genetics, Bioinformatics or in a
related field (A Ph.D qualification would be an advantage).
. Proven 3+ years of experience in similar role.
. Highly proficient in Python, SQL, MySQL.
. Excellent knowledge of mammalian genomics, bioinformatics and
statistical/population genetics.
. Hands-on experience working with large data sets.
. Experience with front-end technologies (HTML/CSS/Javascript) an
advantage.
. Experience in rapid web application development: e.g. Django.
. Knowledge or experience of Unix Scripting and R statistical
programming language would be an advantage.
. Ability to work with minimum supervision to deliver high-quality
code on time.
. Fluency in English and good written and communication skills.
. Meticulous attention to detail.

Applications should be submitted before Friday, 26 September 2014 using the
following link:
http://bit.ly/WgbhxS

Note: Full information and application procedure is available at this link:
http://bit.ly/WgbhxS

3D-Dock Suite

Global rigid search: FFTShape complementarity and electrostatics

Re-scoring and clustering. Refinement of interface side-chains

3D-Garden

Global rigid search in ensamble

Shape complementarity and Lennard–Jones potential

Side chain and backbone dihedral refinement

DOT

Global rigid search: FFTShape complementarity, electrostatics and VDWNone

Escher NG

Global rigid searchShape complementarity, hydrogen bonds and electrostatic

Integrated in VEGA

GRAMM 

Global rigid search: FFT. smooth protein surface representation for soft docking

Shape complementarity and Lennard-Jones potential

Clustering of conformations

GRAMM-X 

Global rigid search: FFT. smooth protein surface representation for soft docking

Shape complementarity and Lennard-Jones potentialminimization and re-scoring with multiple filters

HEX

Global rigid search: Fourier correlation of spherical harmonics

Shape complementarity

HADDOCK

Global rigid searchElectrostatic ,VDW and desolvation energy termsMD simulated annealing refinement . Filtering based on external data. 

ICM

Global rigid search: Monte CarloEmpirical scoring function

Clustering and selection of conformations. Refinement of interface side-chains and re-scoring

MolFit 

Global rigid search: FFTShape complementarity

Clustering of good solutions, filtering using a priori information and small, local rigid rotations around selected conformations

PatchDock

Global rigid searchShape complementarity and atomic desolvation energy

Clustering of conformations

PyDock

Global rigid search:FFTShape complementarity

rescoring by binding electrostatics and desolvation energy

RosettaDock

Local rigid search: Monte Carlo with low and high resolution structure representation levels

Different scoring parameters for the different resolutions 

ZDOCK

Global rigid search: FFTShape complementarity, desolvation energy, and electrostatics.

Energy minimization and re-scoringFree for academics

Point to note:

The proper treatment of flexibility in protein–protein docking is still an active field of research. You first should analyzed your proteins in order to define their conformational space and then choose the most suitable method for your docking problem.

Eligibility:
M.Sc. in any stream of Life Sciences with minimum 55% marks.

Desirable:
Candidates having experience in Molecular Spectroscopy, Protein Folding and Bioinformatics will be preferred.

Interested candidate may appear in the walk in Interview conducted on September 16, 2014 (Tuesday) 11:00 AM in the Director's Office, Centre for Interdisciplinary Research in Basic Sciences, lamia Millia Islamia, New Delhi-110025.
Candidates are required to bring a set of Xerox copy of their recent CV and qualifying degree (certificate/mark sheet) along with original documents. NoTA/DA will be paid.

For any further information you may e-mail to: mihassan@jmLac.in

Read more at http://jmi.ac.in/upload/advertisement/jobs_cirbs_2014september8.pdf