Selective transport of radio-cesium by supported liquid membranes containing calix[4]crown-6 ligands as the mobile carrier

Facilitated transport of Cs-137 across supported liquid membranes (SLM) containing a calix-crown ligand viz. caliz[4]arene-bis(crown-6) (CC), calix[4]arene-bis(o-benzocrown-6) (CBC) or calix[4]arene-bis(napthocrown-6) (CNC) was investigated. The feed consisted of dilute nitric acid solutions while the carrier solutions contained mainly CNC in several organic diluents inside the pores of polypropylene (PP) as well as PTFE flat sheet membranes. PTFE membranes containing CNC in a diluent mixture of 2-nitrophenyloctyl ether (NPOE) and n-dodecane were found to have high stability. Selectivity studies were carried out using simulated high level waste (SHLW) as well as fission products obtained from an irradiated natural uranium target.     

Energy efficient design and occupant well-being: Case studies in the UK and India

The purpose of this paper is to demonstrate the relationships between sustainable building design and occupant well-being. It starts with a definition of sustainable design and well-being, and focuses on the relationships between energy performance and occupant feedback. Methodologically it draws on detailed monitoring and surveys of 12 case study office buildings in the UK and India, and the paper uses the data to explore whether energy use and associated CO₂ emissions are correlated to occupant satisfaction and comfort. The results demonstrate that increased energy use in the case study buildings is associated with increased mechanisation (e.g. centralised air conditioning) and reduced occupant control. This reduced control in turn is shown to relate to reduced occupant comfort and satisfaction. Finally, the paper reveals that the reported health conditions of occupants correlates strongly with their levels of satisfaction. The overall conclusion is that energy use in typical office buildings is inversely correlated with the well-being of the occupants: more energy use does not improve well-being.     

Dynamics study on the anti-human immunodeficiency virus chemokine viral macrophage-inflammatory protein-II (VMIP-II) reveals a fully monomeric protein

Encoded by Kaposi's sarcoma-associated herpesvirus, viral macrophage-inflammatory protein-II (VMIP-II) is unique among CC chemokines in that it has been shown to bind to the CXC chemokine receptor CXCR4 as well as to a variety of CC chemokine receptors. This unique binding ability allows vMIP-II to block infection by a wide range of human immunodeficiency virus type I (HIV-1) strains, but the structural and dynamic basis for this broad range of binding is not known. 15N T1, T2 and 15N[-HN] nuclear Overhauser effect (NOE) values of vMIP-II, determined through a series of heteronuclear multidimensional nuclear magnetic resonance (NMR) experiments, were used to obtain information about the backbone dynamics of the protein. Whereas almost all chemokine structures reveal a dimer or multimer, vMIP-II has a rotational correlation time (tauc) of 4.7 +/- 0.3 ns, which is consistent with a monomeric chemokine. The rotational diffusion anisotropy, D parallel/D perpendicular, is approximately 1.5 +/- 0.1. The conformation of vMIP-II is quite similar to other known chemokines, containing an unstructured N-terminus followed by an ordered turn, three beta-strands arranged in an antiparallel fashion, and one C-terminal alpha-helix that lies across the beta-strands. Most of the protein is well-ordered on a picosecond time scale, with an average order parameter S2 (excluding the N-terminal 13 amino acids) of 0.83 +/- 0. 09, and with even greater order in regions of secondary structure. The NMR data reveal that the N-terminus, which in other chemokines has been implicated in receptor binding, extends like a flexible tail in solution and possesses no secondary structure. The region of the ordered turn, including residues 25-28, experiences conformational exchange dynamics. The implications of these NMR data to the broad receptor binding capability of vMIP-II are discussed.     

The DNA binding properties of Saccharomyces cerevisiae Rad51 protein

Saccharomyces cerevisiae Rad51 protein is the paradigm for eukaryotic ATP-dependent DNA strand exchange proteins. To explain some of the unique characteristics of DNA strand exchange promoted by Rad51 protein, when compared with its prokaryotic homologue the Escherichia coli RecA protein, we analyzed the DNA binding properties of the Rad51 protein. Rad51 protein binds both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) in an ATP- and Mg2+-dependent manner, over a wide range of pH, with an apparent binding stoichiometry of approximately 1 protein monomer per 4 (+/-1) nucleotides or base pairs, respectively. Only dATP and adenosine 5'-gamma-(thiotriphosphate) (ATPgammaS) can substitute for ATP, but binding in the presence of ATPgammaS requires more than a 5-fold stoichiometric excess of protein. Without nucleotide cofactor, Rad51 protein binds both ssDNA and dsDNA but only at pH values lower than 6.8; in this case, the apparent binding stoichiometry covers the range of 1 protein monomer per 6-9 nucleotides or base pairs. Therefore, Rad51 protein displays two distinct modes of DNA binding. These binding modes are not inter-convertible; however, their initial selection is governed by ATP binding. On the basis of these DNA binding properties, we conclude that the main reason for the low efficiency of the DNA strand exchange promoted by Rad51 protein in vitro is its enhanced dsDNA-binding ability, which inhibits both the presynaptic and synaptic phases of the DNA strand exchange reaction as follows: during presynapsis, Rad51 protein interacts with and stabilizes secondary structures in ssDNA thereby inhibiting formation of a contiguous nucleoprotein filament; during synapsis, Rad51 protein inactivates the homologous dsDNA partner by directly binding to it.