Do exons code for structural or functional units in proteins?

In considering the origin and evolution of proteins, the possibility that proteins evolved from exons coding for specific structure-function modules is attractive for its economy and simplicity but is not systematically supported by the available data. However, the number of correspondences between exons and units of protein structure-function that have so far been identified appears to be greater than expected by chance alone. The available data also show (i) that exons are fairly limited in size but are large enough to specify structure-function modules in proteins; (ii) that the position of introns for homologous domains in the same gene is reasonably stable, but there is also evidence for mechanisms that alter the position or existence of introns; and (iii) that it is possible that the observed relationship of exons to protein structure represents a degenerate state of an ancestral correspondence between exons and structure-function modules in proteins

4-(3-Azaniumylpropyl)morpholin-4-ium chloride hydrogen oxalate: An unusual example of a dication with different counter-anions

© 2014 International Union of Crystallography. The mixed organic-inorganic title salt, C7H18N2O2+·C2HO4-·Cl-, forms an assembly of ionic components which are stabilized through a series of hydrogen bonds and charge-assisted intermolecular interactions. The title assembly crystallizes in the monoclinic C2/c space group with Z = 8. The asymmetric unit consists of a 4-(3-azaniumylpropyl)morpholin-4-ium dication, a hydrogen oxalate counter-anion and an inorganic chloride counter-anion. The organic cations and anions are connected through a network of N - H⋯O, O - H⋯O and C - H⋯O hydrogen bonds, forming several intermolecular rings that can be described by the graph-set notations R33(13), R21(5), R12(5), R21(6), R23(6), R22(8) and R33(9). The 4-(3-azaniumylpropyl)morpholin-4-ium dications are interconnected through N - H⋯O hydrogen bonds, forming C(9) chains that run diagonally along the ab face. Furthermore, the hydrogen oxalate anions are interconnected via O - H⋯O hydrogen bonds, forming head-to-tail C(5) chains along the crystallographic b axis. The two types of chains are linked through additional N - H⋯O and O - H⋯O hydrogen bonds, and the hydrogen oxalate chains are sandwiched by the 4-(3-azaniumylpropyl)morpholin-4-ium chains, forming organic layers that are separated by the chloride anions. Finally, the layered three-dimensional structure is stabilized via intermolecular N - H⋯Cl and C - H⋯Cl interactions

Purine nucleoside phosphorylase. Allosteric regulation of a dissociating enzyme.

Purine nucleoside phosphorylase (EC 2.4.2.1) from bovine spleen is a trimeric enzyme that readily dissociates to the monomer. Dilution of enzyme from 20 to 0.02 microgram of protein/ml is accompanied by a greater than 50-fold increase in the specific activity (vtrimer = 0.23 nmol/min/microgram; vmonomer = 12.5 nmol/min/micrograms). Gel permeation chromatography in the presence of the substrate phosphate shows the enzyme to be predominantly trimeric at 50 mM Pi and predominantly monomeric at 100 mM Pi, when experiments are done at 24 degrees C. No significant dissociation was observed at 4 degrees C with Pi or at either temperature with the substrate inosine. As measured by dissociation, the L0.5 for Pi is 88 mM and thus significantly higher than the Km of 3.1 mM for Pi. Enzyme activity as a function of phosphate concentration showed negative cooperativity, but the conformational response measured by the change in native Mr during dissociation showed positive cooperatively toward Pi. These data support a model for two separate phosphate binding sites on the enzyme. The activity and stability of purine nucleoside phosphorylase are quite sensitive to the concentration of the enzyme as well as appropriate substrates. Although the monomer is interpreted as being a fully active form of the enzyme, the data in general are most consistent with the enzyme functioning in vivo as a regulated trimer

The Chemistry of the Reaction Determines the Invariant Amino Acids during the Evolution and Divergence of Orotidine 5′-Monophosphate Decarboxylase

Orotidine 5'-phosphate (OMP) decarboxylase has the largest rate enhancement for any known enzyme. For an average protein of 270 amino acids from more than 80 species, only 8 amino acids are invariant, and 7 of these correspond to ligand-binding residues in the crystal structures of the enzyme from four species. It appears that the chemistry required for catalysis determines the invariant residues for this enzyme structure. A motif of three invariant amino acids at the catalytic site (DXKXXD) is also found in the enzyme hexulose-phosphate synthase. Although the core of OMP decarboxylase is conserved, it has undergone a variety of changes in subunit size or fusion to other protein domains, such as orotate phosphoribosyltransferase, during evolution in different kingdoms. The phylogeny of OMP decarboxylase shows a unique subgroup distinct from the three kingdoms of life. The enzyme subunit size almost doubles from Archaea (average mass of 24.5 kDa) to certain fungi (average mass of 41.7 kDa). These observed changes in subunit size are produced by insertions at 12 sites, largely in loops and on the exterior of the core protein. The consensus for all sequences has a minimal size of <20 kDa

Solution processed amorphous silicon surface passivation layers

Amorphous silicon thin films, fabricated by thermal conversion of neopentasilane, were used to passivate crystalline silicon surfaces. The conversion is investigated using X ray and constant final state yield photoelectron spectroscopy, and minority charge carrier lifetime spectroscopy. Liquid processed amorphous silicon exhibits high Urbach energies from 90 to 120 meV and 200 meV lower optical band gaps than material prepared by plasma enhanced chemical vapor deposition. Applying a hydrogen plasma treatment, a minority charge carrier lifetime of 1.37 ms at an injection level of 1015 cm3 enabling an implied open circuit voltage of 724 mV was achieved, demonstrating excellent silicon surface passivatio

CO2 Targets, Trajectories and Trends for International Shipping

The Shipping in Changing Climates (SCC) project connects the latest climate change science with knowledge, understanding and models of the shipping sector in a whole systems approach. It seeks to explore the potential to cut CO2 through the use of technical and operational changes in shipping and to understand how the sector might transition to a more resilient and low-carbon future; it also seeks to explore different climate change scenarios and related food and fuel security issues to gain an understanding of the direct and indirect impacts of climate change on the shipping sector. These scenarios can be used to build evidence and understanding around the range of potential future directions that the shipping industry may take. The RCUK Energy funded project brings together researchers from UCL (Energy Institute, Mechanical Engineering and Laws), Manchester, Southampton, Newcastle and Strathclyde, in close collaboration with a core industry stakeholder group of Shell, Lloyd’s Register, Rolls Royce, BMT and Maritime Strategies International, but drawing on the expertise and connections of over 35 companies and organisations worldwide. This paper is non-peer- reviewed and represents the collective opinions of the authors and should not be assumed to represent the views of all the researchers across the project or the project’s industry partners and their organisations

Uridine kinase from Ehrlich ascites carcinoma. Purification and properties of homogeneous enzyme.

Uridine kinase from Ehrlich ascites tumor cells has been purified about 60,000-fold to apparent homogeneity and with an overall recovery of about 40%. This purification was achieved using phosphocellulose and adenosine 5'-triphosphate-agarose affinity chromatography. The subunit molecular mass as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was 31,000 daltons. With two-dimensional electrophoresis, only one spot was observed, indicating the absence of isoenzymes. Multiple peaks of activity are routinely observed on ion exchange chromatography or gel filtration, for both crude preparations or homogeneous uridine kinase, in agreement with our earlier results that this enzyme exists as multiple interconvertible oligomeric forms (Payne, R. C., and Traut, T. W. (1982) J. Biol. Chem. 257, 12485-12488). The purified enzyme has a specific activity of 283 mumol/min/mg of protein at 22 degrees C. Initial velocity studies using uridine and ATP are consistent with a sequential mechanism. Km values for uridine, cytidine, and ATP are 40, 57, and 450 microM, respectively. CTP and UTP are competitive inhibitors with respect to ATP, with Ki values for CTP and UTP of 10 and 61 microM, respectively. The enzyme was active with several nucleoside analogs, the Km values being 69 microM (5-fluorouridine), 200 microM (3-deazauridine), and 340 microM (6-azauridine). The pure enzyme is very sensitive to freezing, but can be maintained at O degrees C for 8 weeks with only 20% loss of activity. For long-term storage, enzyme in 50% glycerol can be maintained at -20 degrees C for many months with no detectable loss of activity

A Test of Kangaroo Care on Preterm Infant Breastfeeding

To test the effects of kangaroo care (KC) on breastfeeding outcomes in preterm infants compared to two control groups and to explore whether maternal-infant characteristics and the mother’s choice to use KC were related to breastfeeding measures

Design and Synthesis of a Novel Alpha-Methylene Lactone Chemotherapeutic Agent

Goniothalamin, a natural product isolated from the dried stem bark of Malaysian plants of the genus Goniothalamus, has been shown to induce apoptosis in cancer cells. The bioactivity of this molecule is though to be due to its ability to react with thiols. One mechanism involves its reaction with glutathione, a natural antioxidant found in all cells. Using a four step synthetic sequence, a novel gamma-lactone analogue of goniothalamin has been prepared that replaces the endocylic double bond in goniothalamin\u27s lactone core with an exocyclic double bond. It is anticipated that this alteration will allow the compound to react more rapidly with thiols and therefore increase its cytotoxicity towards cancer cells

CO2 abatement goals for international shipping

The Paris Agreement, which entered into force in 2016, sets the ambitious climate change mitigation goal of limiting the global temperature increase to below 2°C and ideally 1.5°C. This puts a severe constraint on the remaining global GHG emissions budget. While international shipping is also a contributor to anthropogenic GHG emissions, and CO2 in particular, it is not included in the Paris Agreement. This article discusses how a share of a global CO2 budget over the twenty-first century could be apportioned to international shipping, and, using a range of future trade scenarios, explores the requisite cuts to the CO2 intensity of shipping. The results demonstrate that, under a wide range of assumptions, existing short-term levers of efficiency must be urgently exploited to achieve mitigation commensurate with that required from the rest of the economy, with virtually full decarbonization of international shipping required as early as before mid-century