Analysis of Organophosphorus Compounds. 1. Application of Iodine-Azide Reaction for Detection of Thiophosphoorganic Compounds in Thin-Layer Chromatography

Wydrukowano z dostarczonych Wydawnictwu UŁ gotowych materiałówZadanie pt. Digitalizacja i udostępnienie w Cyfrowym Repozytorium Uniwersytetu Łódzkiego kolekcji czasopism naukowych wydawanych przez Uniwersytet Łódzki nr 885/P-DUN/2014 zostało dofinansowane ze środków MNiSW w ramach działalności upowszechniającej naukę

Draft genome sequence of MCPA-degrading <i>Sphingomonas </i>sp. strain ERG5, isolated from a groundwater aquifer in Denmark

Sphingomonas sp. strain ERG5 was isolated from a bacterial community, originating from a groundwater aquifer polluted with low pesticide concentrations. This bacterium degrades 2-methyl-4-chlorophenoxyacetic acid (MCPA) in a wide spectrum of concentrations and has been shown to function in bioaugmented sand filters. Genes associated with MCPA degradation are situated on a putative conjugative plasmid

Lipid-induced changes in the secondary structure of snake venom cardiotoxins.

The secondary structures of three snake venom cardiotoxins (from Hemachatus hemachatus, Naja naja atra, and Naja naja naja), in aqueous solution and in a lipid-bound form, were investigated by Fourier-transform infrared spectroscopy. The conformation-sensitive protein infrared bands in the amide I region were analyzed using deconvolution and band-fitting procedures. The spectra of the three cardiotoxins in aqueous buffer are very similar; they indicate a high content of both antiparallel beta-sheet structure and unordered conformation. Moreover, component bands characteristic of turns can also be identified. The binding of cardiotoxins to bilayers of dimyristoylphosphatidyl-glycerol results in an increased content of a beta-structure at the expense of the nonordered conformation. It is suggested that lipid-induced conformational transitions to a beta-structure, similar to that observed with cardiotoxins, may be operative also in membrane interaction of other proteins and peptides, particularly with those which have a small tendency to form alpha-helices

Ultra high purity, dimensionally stable INVAR 36

An INVAR 36 material having long-term dimensional stability is produced by sintering a blend of powders of nickel and iron under pressure in an inert atmosphere to form an alloy containing less than 0.01 parts of carbon and less than 0.1 part aggregate and preferably 0.01 part individually of Mn, Si, P, S and Al impurities. The sintered alloy is heat treated and slowly and uniformly cooled to form a material having a coefficient of thermal expansion of less than 1 ppm/C and a temporal stability of less than 1 ppm/year

Hierarchical assembly of an interlocked M8L16 container

The self‐assembly of eight PdII cations and sixteen phenanthrene‐derived bridging ligands with 60° bite angles yielded a novel M8L16 metallosupramolecular architecture composed of two interlocked D4h‐symmetric barrel‐shaped containers. Mass spectrometry, NMR spectroscopy, and X‐ray analysis revealed this self‐assembled structure to be a very large “Hopf link” catenane featuring channel‐like cavities, which are occupied by NO3− anions. The importance of the anions as catenation templates became imminent when we observed the nitrate‐triggered structural rearrangement of a mixture of M3L6 and M4L8 assemblies formed in the presence of BF4− anions into the same interlocked molecule. Furthermore, the densely packed structure of the M8L16 catenane was exploited in the preparation of a hexyloxy‐functionalized analogue, which further self‐assembled into vesicle‐like aggregates in a reversible manner

Morphological control of heteroleptic cis- and trans-Pd2L2Lʹ2 cages

Control over the integrative self-sorting of metallo-supramolecular assemblies has recently generated significant interest as it opens up possibilities of introducing increased complexity and function into a single self-assembled architecture. Here, the relationship between the geometry of three ligand components and morphology of three self-sorted heteroleptic [Pd2L2Lʹ2]4+ cages is examined. Pd-mediated assembly of two bis-monodentate pyridyl ligands with native bite angles of 75° and 120° affords a cis-[Pd2L2Lʹ2]4+ cage while the same reaction with two ligands bearing bite angles of 75° and 60° forces an anti-conformation for latter ligand, leading to an unprecedented, self-penetrating structural motif; a trans-[Pd2(anti-L)2Lʹ2]4+ heteroleptic cage bearing a “doubly-bridged figure-eight” topology. Each heteroleptic assembly can be accessed through cage-to-cage conversion of their homoleptic precursors, and notably, morphological control of [Pd2L2Lʹ2] cages is achieved through selective ligand displacement transformations in a system of three ligands and at least six possible cage products

pH-dependent Stability and Membrane Interaction of the Pore-forming Domain of Colicin A*

Thermal stability of the pore-forming domain of colicin A was studied by high sensitivity differential scanning calorimetry and circular dichroism spectroscopy. In the pH range between 8 and 5, the thermal denaturation of the protein in solution occurs at 66-69 degrees C and is characterized by the calorimetric enthalpy of approximately 90 kcal/M. At pH below 5, there is a rapid pH-dependent destabilization of the pore-forming domain resulting in the lowering of the midpoint denaturation temperature and a decrease in the calorimetric enthalpy of denaturation. Circular dichroism spectra in the near and far ultraviolet show that the thermotropic transition is associated with collapse of the native tertiary structure of the pore-forming domain, although a large proportion of the helical secondary structure remains preserved. The present data indicate some similarity also between acid-induced and temperature-induced denaturation of the pore-forming domain of colicin A. Association of the pore-forming domain with phospholipid vesicles of dioleoylphosphatidylglycerol results in total disappearance of the calorimetric transition, even at pH values as high as 7. Since lipid binding also induces collapse of the near ultraviolet circular dichroism spectrum, these data indicate that interaction with the membrane facilitates a conformational change within the pore-forming domain to a looser (denaturated-like) state. These findings are discussed in relation to the recent model (van der Goot, F. G., Gonzalez-Manas, J. M., Lakey, J. H., Pattus, F. (1991) Nature 354, 408-410) which postulates that a flexible "molten globule" state is an intermediate on the pathway to membrane insertion of colicin A

Draft Genome Sequence of Se(IV)-Reducing Bacterium Pseudomonas migulae ES3-33

Pseudomonas migulae ES3-33 is a Gram-negative strain that strongly reduces Se(IV) and was isolated from a selenium mining area in Enshi, southwest China. Here we present the draft genome of this strain containing potential genes involved in selenite reduction and a large number of genes encoding resistances to copper and antibiotics