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).

Research Associate Biotechnology /JRF / Lab. Assistant recruitment in Indian Institute of Vegetable Research

Project:
Genomics assisted selection of Solanum chilense introgression lines for enhancing drought tolerance in tomato
Post Name : Research Associate
Qualification : Ph.D in Biotechnology/ Bioinformatics/Genetics & Plant Breeding. M. Tech in Computer Science with at least one research paper in science citation indexed journal. Desirable: Experience in bioinformatics and next generation sequence data handling. Familiarity in Linux, R, Perl/Phython or other programming languages. Willingness to travel to European partner centers.

Pay Scale : Rs. 36000 for 1st and 2nd year as per rules for Research Associate. Rs. 25000/- for 1st and 2nd year and Rs. 28000 as per rules for Junior Research Fellow. Rs. 7000/- for Lab. Assistant.

Age : Not more than 35 years for Men and 40 years for Women (Relaxable for SC/ST/OBC/PH candidates as per rules) for Research Associate/ Junior Research Fellow. Minimum age will be 21 years and maximum age will be 45 years (Relaxable for SC/ST/OBC/PH candidates as per rules) for Lab.Assistant.

More at http://iivr.org.in/Job%20Oppurtunities/RA20.03.2015.pdf

The standalone version (Linux-based command-line) of RNAcon is freely available for the global scientific community.

Reference: Panwar, B.; Arora, A. and Raghava, G.P.S. (2014) Prediction and classification of ncRNAs using structural informationBMC Genomics 2014, 15:127

Address of the bookmark: http://crdd.osdd.net/raghava/rnacon/

A walk-in-Interview is proposed to be held at National Bureau of Animal Genetic Resources, Karnal (Haryana)-132001 at 10:30 AM on 19.08.2015 to select One Research Associate & Three Senior Research Fellow as per details given below:

Name of the project & project period: ICAR Consortium Platform on Genomics.

The post duration is Upto 31.03.2017 or earlier & Co-terminus with the project.

Upto 31.03.2017 or earlier and Coterminus with the project

Essential Qualifications: PhD degree in Bioinformatics OR Master’s degree in Bioinformatics with 4 years/5 years of Bachelor’s degree having 1st division or 60% marks or equivalent overall grade point average, with at least two years of research experience as evidenced from Fellowship/Associateship

Desirable: Working experience in Next Generation Sequencing data analysis

Emolument: Research Associates may be fixed at a consolidated amount at one of the two pay levels given below depending upon the qualification & experience.

I. Research Associate – Master Degree Holders Rs. 38,000/ + HRA II. Research Associate – Doctoral Degree Holder Rs. 40,000/ + HRA

Senior Research Fellow: Two:- Bioinformatics One: - Biotechnology.

Duration of engagement: Upto 31.03.2017 or earlier and Coterminus with the project

Essential Qualifications: Master degree in any one of discipline/ Subjects- Biotechnology/Bioinformatics with 4 years/5 years of Bachelor’s degree.

Candidates having post graduate degree in above mentioned subjects with 3 years Bachelor’s degree should have NET qualification.

Desirable: The candidates should have zeal to work in R environment and NGS data analysis Emolument: Rs. 28,000/- per month + HRA as per admissibility

Age Limit: 1. 40 year for Men and 45 years for Women in case of RA on the date of Interview. 2. 35 year for Men and 40 years for Women in case of SRF on the date of Interview. (Relaxation for SC/ST/OBC and PHC as per GOI/ICAR rules) The above positions are purely temporary and will be filled in on Contractual basis. The selected candidate shall have no right/claim for regular appointment at this Institute, as the engagement is co-terminus with the Project/Scheme.

Interested candidates may attend Walk-in-Interview at 10:30 AM on 19.08.2015 alongwith original certificates and typed bio-data with one set of attested copies of each their certificates with passport size photograph. No TA/DA will be paid for attending the interview. All eligible candidates are advised to be present at least 30 minutes before scheduled time on the date of interview for completing necessary formalities. Canvassing in any form will disqualify the candidates.

More at http://210.212.93.85/Advertisiment3.pdf

No of Post: 01
How To Apply: Walk-in interview will be held on 24-03-2015 at 10:00 AM at NRCPB, New Delhi for filling Research Associate and Senior Research Fellow positions as mentioned below. The positions are temporary and are initially offered for a period of one year. Details such as emoluments, qualifications, application format etc., are given below. Desirous candidates should report for interview latest by 10:30 AM with the application in the prescribed format, copies and originals of certificates, thesis and documents. No TA/DA will be provided for attending the interview
General Instructions: The positions are purely temporary, on a contractual basis and are initially offered for one year. The period and duration of the scheme is tentative and the same may change. The person employed will have no right to claim employment or engagement in ICAR at the end of the contract period. No TA/DA will be provided for appearing in the interview. Persons already in employment should bring “No Objection Certificate” from their present employer. The candidates must bring with them five copies of the CV in the format given below along with original documents such as t h e s i s , degree certificates, marks sheets, publications, experience certificate etc. for verification and one set of self attested copy of all certificates. The decision of the Project Director of this Institute will be final and binding in all aspects. In case of any disputes, it will be resolved within the jurisdiction of New Delhi Court only.
Detail of Interview: 24-03-2015
Age Limit: 35 Years
Contact Details: Ph: 011-25848783; Fax: 25843984

NIPGR is commonly known as National Institute of Plant Genome Research. Recently, it’s great opportunity for those candidates who are interested to do job in NIPGR. National Institute of Plant Genome Research (NIPGR) had found to build a bridge between the branches of natural sciences and due this connection it is steeping on the heaps of success. Its objectives to preserve, research, production and the advancement in the trait are very clear and also being appreciated by the nation and had been contributing for the further enrichment of the institute. NIPGR had announced the recruitment to further make improvements and amendments by the young potential in their panel. The recruitment is being announced for the post is mentioned below. We are giving a complete information to applicants for find their eligibility as per desired post under NIPGR Recruitment 2015 project but if the candidates are not satisfied with this information then they can download an official advertisement of NIPGR recruitment 2015 from the link defined ahead under the head of reference.

NIPGR Recruitment 2015 for the 1 post of Research Associate: National Institute of Plant Genome Research (NIPGR) had instigated the progression of the recruitment and this process is linked thoroughly so as the 1 post of Research Associate. Applicants are associated and linked with the education to be PHD degree in the life science, biotechnology, bioinformatics or molecular biology. Applicants are associated with the dispatch of the application along with the required certificates so as on the date of 24th Feb 2015.

The recruitment notification and application @ http://www.nipgr.res.in/careers/vacancies_latest.php#

More at http://bcil.nic.in/default.htm

Vacancies:
Research Associate-02
Age Limits:
Candidates age limit should be not more than 40 years as on date of interview.
Qualification:
Candidates should possess Ph.D in Bioinformatics/Agricultural Statistics/Statistics/Computer Science/Computer Application or equivalent.
Selection Process:
Selection will be based on interview.
How to Apply:
Eligible candidates may attend for interview along with application in prescribed format, recent passport size photograph pasted on the application form, bio-data, original certificates and self attested copies of relevant documents, all experience certificates, testimonials etc, held at Indian Agricultural Statistics Research Institute, Pusa, New Delhi on 18-04-2015 at 10:30 AM.
Last Date:
18-04-2015