A New Approach to Tagging Data in the Astronomical Literature

Data Tags are strings used in journals to indicate the origin of the archival data and to enable the reader to recover the data. The NASA/IPAC Infrared Science Archive (IRSA) has recently introduced a new approach to production of data tags and recovery of data from them. Many of the data access services at the IRSA return filtered data sets (such as subsets of source catalogs) and dynamically created products (such as image cutouts); these dynamically created products are not saved permanently at the archive. Rather than tag the data sets from which the query result sets are drawn, the archive tags the query that generates the results. A single tag can, then, encode a complex dynamic data set and simplifies the embedding of tags in manuscripts and journals. By logging user queries and all the parameters for those query as Data Tags, IRSA can re-create the query and rerun the IRSA service using the same search parameters used when the Data Tag was created. At the same time, the logs give a simple count of the actual numbers of queries made to the archive, a powerful metric of archive usage unobtainable from the Apache web server logs. Currently, IRSA creates tags for queries to more than 20 data sets, including the Infrared Astronomical Satellite (IRAS), Cosmic Evolution Survey (COSMOS) and Spitzer Space Telescope Legacy Data Sets. These tags are returned by the spatial query engine, Atlas. IRSA plans to create tags for queries to the rest of its services in late Spring 2007. The archive provides a simple web interface which recovers a data set that corresponds to the input data tag. Archived data sets may evolve in time due to improved calibrations or augmentations to the data set. IRSA’s query based approach guarantees that users always receive the best available data sets

Spitzer data at the NASA/IPAC Infrared Science Archive (IRSA)

The NASA/IPAC Infrared Science Archive (IRSA) curates and serves science data sets from NASA’s infrared and submillimeter projects and missions, including IRAS, 2MASS, MSX, SWAS, ISO, IRTS and from the Spitzer Space Telescope. All Spitzer data can be accessed from IRSA’s Spitzer mission page at: http://irsa.ipac.caltech.edu/Missions/spitzer.html Spitzer Legacy Enhanced Products along with ancillary data are delivered in six month intervals starting from Fall 2004, until Fall 2006. IRSA continually ingests the Spitzer data and the ancillary data, and these data are made accessible through IRSA’s query engines. Legacy products for the C2D, FEPS, GLIMPSE, GOODS, SINGS and SWIRE projects are accessible through a common interface http://irsa.ipac.caltech.edu/applications/Atlas. This engine returns the spatial footprints of observations and provides access to all flavors of released data sets, including, where appropriate, previews of image mosaics, 3-color image mosaics and spectra

On the pH-optimum of Activity and Stability of Proteins

Biological macromolecules evolved to perform their function in specific cellular environment (subcellular compartments or tissues); therefore, they should be adapted to the biophysical characteristics of the corresponding environment, one of them being the characteristic pH. Many macromolecular properties are pH dependent, such as activity and stability. However, only activity is biologically important, while stability may not be crucial for the corresponding reaction. Here, we show that the pH-optimum of activity (the pH of maximal activity) is correlated with the pH-optimum of stability (the pH of maximal stability) on a set of 310 proteins with available experimental data. We speculate that such a correlation is needed to allow the corresponding macromolecules to tolerate small pH fluctuations that are inevitable with cellular function. Our findings rationalize the efforts of correlating the pH of maximal stability and the characteristic pH of subcellular compartments, as only pH of activity is subject of evolutionary pressure. In addition, our analysis confirmed the previous observation that pH-optimum of activity and stability are not correlated with the isoelectric point, pI, or with the optimal temperature

Observing pulsars and fast transients with LOFAR

Low frequency radio waves, while challenging to observe,are a rich source of information about pulsars. The LOw Frequency ARray (LOFAR) is a new radio interferometer operating in the lowest 4 octaves of the ionospheric “radio window”: 10–240 MHz, that will greatly facilitate observing pulsars at low radio frequencies. Through the huge collecting area, long baselines, and flexible digital hardware, it is expected that LOFAR will revolutionize radio astronomy at the lowest frequencies visible from Earth.LOFAR is a next-generation radio telescope and a pathfinder to the Square Kilometre Array (SKA), in that it incorporates advanced multi-beaming techniques between thousands of individual elements. We discuss the motivation for low-frequency pulsar observations in general and the potential of LOFAR in addressing these science goals.We present LOFAR as it is designed to perform high-time-resolution observations of pulsars and other fast transients, and outline the various relevant observing modes and data reduction pipelines that are already or will soon be implemented to facilitate these observations. A number of results obtained from commissioning observations are presented to demonstrate the exciting potential of the telescope. This paper outlines the case for low frequency pulsar observations and is also intended to serve as a reference for upcoming pulsar/fast transient science papers with LOFAR

PROTCOM: searchable database of protein complexes enhanced with domain–domain structures

The database of protein complexes (PROTCOM) is a compilation of known 3D structures of protein–protein complexes enriched with artificially created domain–domain structures using the available entries in the Protein Data Bank. The domain–domain structures are generated by parsing single chain structures into loosely connected domains and are important features of the database. The database () could be used for benchmarking purposes of the docking and other algorithms for predicting 3D structures of protein–protein complexes. The database can be utilized as a template database in the homology or threading methods for modeling the 3D structures of unknown protein–protein complexes. PROTCOM provides the scientific community with an integrated set of tools for browsing, searching, visualizing and downloading a pool of protein complexes. The user is given the option to select a subset of entries using a combination of up to 10 different criteria. As on July 2006 the database contains 1770 entries, each of which consists of the known 3D structures and additional relevant information that can be displayed either in text-only or in visual mode

Electrostatic Properties of Protein-Protein Complexes

Statistical electrostatic analysis of 37 protein-protein complexes extracted from the previously developed database of protein complexes (ProtCom, http://www.ces.clemson.edu/compbio/protcom) is presented. It is shown that small interfaces have a higher content of charged and polar groups compared to large interfaces. In a vast majority of the cases the average pKa shifts for acidic residues induced by the complex formation are negative, indicating that complex formation stabilizes their ionizable states, whereas the histidines are predicted to destabilize the complex. The individual pKa shifts show the same tendency since 80% of the interfacial acidic groups were found to lower their pKas, whereas only 25% of histidines raise their pKa upon the complex formation. The interfacial groups have been divided into three sets according to the mechanism of their pKa shift, and statistical analysis of each set was performed. It was shown that the optimum pH values (pH of maximal stability) of the complex tend to be the same as the optimum pH values of the complex components. This finding can be used in the homology-based prediction of the 3D structures of protein complexes, especially when one needs to evaluate and rank putative models. It is more likely for a model to be correct if both components of the model complex and the entire complex have the same or at least similar values of the optimum pH

Cytoplasmic dynein binding, run length, and velocity are guided by long-range electrostatic interactions

Dyneins are important molecular motors involved in many essential biological processes, including cargo transport along microtubules, mitosis, and in cilia. Dynein motility involves the coupling of microtubule binding and unbinding to a change in the configuration of the linker domain induced by ATP hydrolysis, which occur some 25 nm apart. This leaves the accuracy of dynein stepping relatively inaccurate and susceptible to thermal noise. Using multi-scale modeling with a computational focusing technique, we demonstrate that the microtubule forms an electrostatic funnel that guides the dynein’s microtubule binding domain (MTBD) as it finally docks to the precise, keyed binding location on the microtubule. Furthermore, we demonstrate that electrostatic component of the MTBD’s binding free energy is linearly correlated with the velocity and run length of dynein, and we use this linearity to predict the effect of mutating each glutamic and aspartic acid located in MTBD domain to alanine. Lastly, we show that the binding of dynein to the microtubule is associated with conformational changes involving several helices, and we localize flexible hinge points within the stalk helices. Taken all together, we demonstrate that long range electrostatic interactions bring a level of precision to an otherwise noisy dynein stepping process

On the Role of Electrostatics in Protein–Protein Interactions

The role of electrostatics in protein–protein interactions and binding is reviewed in this paper. A brief outline of the computational modeling, in the framework of continuum electrostatics, is presented and the basic electrostatic effects occurring upon the formation of the complex are discussed. The effect of the salt concentration and pH of the water phase on protein–protein binding free energy is demonstrated which indicates that the increase of the salt concentration tends to weaken the binding, an observation that is attributed to the optimization of the charge–charge interactions across the interface. It is pointed out that the pH-optimum (pH of optimal binding affinity) varies among the protein–protein complexes, and perhaps is a result of their adaptation to particular subcellular compartments. The similarities and differences between hetero- and homo-complexes are outlined and discussed with respect to the binding mode and charge complementarity

Poisson-Boltzmann Calculations of Nonspecific Salt Effects on Protein-Protein Binding Free Energies

The salt dependence of the binding free energy of five protein-protein hetero-dimers and two homo-dimers/tetramers was calculated from numerical solutions to the Poisson-Boltzmann equation. Overall, the agreement with experimental values is very good. In all cases except one involving the highly charged lactoglobulin homo-dimer, increasing the salt concentration is found both experimentally and theoretically to decrease the binding affinity. To clarify the source of salt effects, the salt-dependent free energy of binding is partitioned into screening terms and to self-energy terms that involve the interaction of the charge distribution of a monomer with its own ion atmosphere. In six of the seven complexes studied, screening makes the largest contribution but self-energy effects can also be significant. The calculated salt effects are found to be insensitive to force-field parameters and to the internal dielectric constant assigned to the monomers. Nonlinearities due to high charge densities, which are extremely important in the binding of proteins to negatively charged membrane surfaces and to nucleic acids, make much smaller contributions to the protein-protein complexes studied here, with the exception of highly charged lactoglobulin dimers. Our results indicate that the Poisson-Boltzmann equation captures much of the physical basis of the nonspecific salt dependence of protein-protein complexation

On the energy components governing molecular recognition in the framework of continuum approaches

Molecular recognition is a process that brings together several biological macromolecules to form a complex and one of the most important characteristics of the process is the binding free energy. Various approaches exist to model the binding free energy, provided the knowledge of the 3D structures of bound and unbound molecules. Among them, continuum approaches are quite appealing due to their computational efficiency while at the same time providing predictions with reasonable accuracy. Here we review recent developments in the field emphasizing on the importance of adopting adequate description of physical processes taking place upon the binding. In particular, we focus on the efforts aiming at capturing some of the atomistic details of the binding phenomena into the continuum framework. When possible, the energy components are reviewed independently of each other. However, it is pointed out that rigorous approaches should consider all energy contributions on the same footage. The two major schemes for utilizing the individual energy components to predict binding affinity are outlined as well