A molecular dynamics study on the thermal rectification effect at the solid–liquid interfaces between the face-centred cubic (FCC) of gold (Au) with the surfaces of (100), (110) and (111) crystal planes facing the liquid methane (CH4)

A molecular dynamics study on the solid–liquid (S-L) interfaces for solid wall of gold having the face-centred cubic of (100), (110) and (111) crystal planes contacting liquid methane was examined using non-equilibrium molecular dynamics simulations. An investigation on the thermal rectification effect was performed by measuring the thermal boundary conductance (TBC) at the S-L interface. Thermal rectification can be defined as the differences in the TBC at the interface between the two opposite heat flow directions; one is from the liquid to solid and vice versa. The thermal rectifications are up to 13% for (110) crystal plane, followed by 6% and 0.3% for (111) and (100) crystal planes, respectively. It was found that the TBC at the S-L interface was influenced by the magnitude of the adsorption of liquid molecules at the vicinity of the interface. The results show that due to the different temperature distribution, different magnitude of the adsorption of liquid molecules is generated for the two opposite heat flow directions. On the surface of the solid walls for (110) crystal plane, where lattice-scale corrugation exists, it was found that there exists difference in distance between the surface layers of the solid and liquid across the interface between the cases of the two opposite heat flow directions, which affects the TBC at the interface. The present results suggest that the factors that influence the thermal rectification at the S-L interface are the magnitude of the adsorption of liquid molecules and the surface structure of the solid walls that differ significantly among the three types of crystal planes.     

Linkage between the loci for the Lp(a) lipoprotein (LP) and plasminogen (PLG)

Summary A locus, LP, that determines quantitative variation of Lp(a) lipoprotein phenotypes is linked to the plasminogen (PLG) locus (peak lod score =12.73). This linkage relationship assigns a locus with alleles that have an affect on risk for coronary artery disease to the long arm of chromosome 6.     

Lipopolysaccharides (LPS) modulate the metabolism of deoxynivalenol (DON) in the pig

Pigs might be exposed to lipopolysaccharides (LPS) and deoxynivalenol (DON) at the same time, and both toxins are thought to interactively affect the intestinal barrier, the innate immune system, and the xenobiotics metabolism. Hence, we aimed at examining the single and combined effects of both toxins on nutrient digestibility and DON metabolism. For this purpose, barrows (26?±?4 kg) were fed restrictedly either a control diet (CON) or a diet contaminated with 3.1 mg DON/kg (DON) for 37 days. At day 37 of the experiment, pigs were infused intravenously for 60 min either with 100 μg DON/kg body weight (BW) (CON-DON), 7.5 μg LPS/kg BW (CON-LPS, DON-LPS) or a combination of both substances (CON-DON?+?LPS), or physiological saline (CON-CON, DON-CON). Blood samples were collected frequently until 3.25 h before the pigs were sacrificed for bile, liver, and kidney collection. The apparent digestibility of N-free extractives was significantly increased by 1 % when the DON-contaminated diet was fed. The total DON content in blood was significantly higher in endotoxemic pigs (34.8 ng/mL; CON-DON?+?LPS) when compared to the pigs infused with DON alone (18.8 ng/mL; CON-DON) while bile concentrations were not influenced by LPS. DON residue levels in liver and kidney closely reflected the treatment effects as described for blood. In contrast to DON infusion, the LPS challenge resulted in a significantly lower total DON concentration (13.2 vs. 7.5 ng/mL in groups DON-CON and DON-LPS, respectively) when the pigs were exposed to DON through the diet. The conjugation degree for DON in blood and bile was not influenced by treatments. In conclusion, endotoxemic pigs are characterized by higher DON residue levels in blood, liver, and kidney, probably by a compromised elimination.     

Mutations in the beta-subunit Thr(159) and Glu(184) of the Rhodospirillum rubrum F(0)F(1) ATP synthase reveal differences in ligands for the coupled Mg(2+)- and decoupled Ca(2+)-dependent F(0)F(1) activities

In the crystal structure of the mitochondrial F(1)-ATPase, the beta-Thr(163) residue was identified as a ligand to Mg(2+) and the beta-Glu(188) as directly involved in catalysis. We replaced the equivalent beta-Thr(159) of the chromatophore F(0)F(1) ATP synthase of Rhodospirillum rubrum with Ser, Ala, or Val and the Glu(184) with Gln or Lys. The mutant beta subunits were isolated and tested for their capacity to assemble into a beta-less chromatophore F(0)F(1) and restore its lost activities. All of them were found to bind into the beta-less enzyme with the same efficiency as the wild type beta subunit, but only the beta-Thr(159) --> Ser mutant restored the activity of the assembled enzyme. These results indicate that both Thr(159) and Glu(184) are not required for assembly and that Glu(184) is indeed essential for all the membrane-bound chromatophore F(0)F(1) activities. A detailed comparison between the wild type and the beta-Thr(159) --> Ser mutant revealed a rather surprising difference. Although this mutant restored the wild type levels and all specific properties of this F(0)F(1) proton-coupled ATP synthesis as well as Mg- and Mn-dependent ATP hydrolysis, it did not restore at all the proton-decoupled CaATPase activity. This clear difference between the ligands for Mg(2+) and Mn(2+), where threonine can be replaced by serine, and Ca(2+), where only threonine is active, suggests that the beta-subunit catalytic site has different conformational states when occupied by Ca(2+) as compared with Mg(2+). These different states might result in different interactions between the beta and gamma subunits, which are involved in linking F(1) catalysis with F(0) proton-translocation and can thus explain the complete absence of Ca-dependent proton-coupled F(0)F(1) catalytic activity.     

On the fauna of chironomidae (Diptera) of the Hrazdan Basin (Armenia)

A faunistic review of larvae and pupae of chironomid midges (Diptera, Chironomidae) from 15 habitats in the Hrazdan River valley (Armenia) is presented. The revealed fauna includes 40 species from 20 genera and 6 families and tribes. Diploid chromosome numbers are specified for 24 species from 13 genera and 4 subfamilies; 23 species from 14 genera and 4 subfamilies are reported from the region for the first time. Predominant oligotrophic status is confirmed for most of the reservoirs studied.     

Characterization of divalent cation localization in the minor groove of the A(n)T(n) and T(n)A(n) DNA sequence elements by (1)H NMR spectroscopy and manganese(II)

The localization of Mn(2+) in A-tract DNA has been studied by (1)H NMR spectroscopy using a series of self-complementary dodecamer oligonucleotides that contain the sequence motifs A(n)(n) and T(n)A(n), where n = 2, 3, or 4. Mn(2+) localization in the minor groove is observed for all the sequences that have been studied, with the position and degree of localization being highly sequence-dependent. The site most favored for Mn(2+) localization in the minor groove is near the 5'-most ApA step for both the T(n)A(n) and the A(n)T(n) series. For the T(n)A(n) series, this results in two closely spaced symmetry-related Mn(2+) localization sites near the center of each duplex, while for the A(n)T(n) series, the two symmetry-related sites are separated by as much as one half-helical turn. The degree of Mn(2+) localization in the minor groove of the T(n)A(n) series decreases substantially as the AT sequence element is shortened from T(4)A(4) to T(2)A(2). The A(n)T(n) series also exhibits length-dependent Mn(2+) localization; however, the degree of minor groove occupancy by Mn(2+) is significantly less than that observed for the T(n)A(n) series. For both A(n)T(n) and T(n)A(n) sequences, the 3'-most AH2 resonance is the least broadened of the AH2 resonances. This is consistent with the observation that the minor groove of A-tract DNA narrows in the 5' to 3' direction, apparently becoming too narrow after two base pairs for the entry of a fully hydrated divalent cation. The results that are reported illustrate the delicate interplay that exists between DNA nucleotide sequence, minor groove width, and divalent cation localization. The proposed role of cation localization in helical axis bending by A-tracts is also discussed.     

(AGCTG) (AGCTG) (AGCTG) (GGGTG) as the primordial sequence of intergenic spacers: the role in immunoglobulin class switch

The means employed for immunoglobulin heavy chain class switch appears to be no different from that by which meiotic intergenic crossing-overs at accomplished. As with other intergenic spacers, the 5' noncoding sequence of each Ig CH (immunoglobulin heavy chain constant region) gene apparently undergoes unconstrained sequence changes due to randomly sustained base substitutions, deletions, and duplications. Yet, there remains sufficient regional sequence homology between the Ig Cmu 5' noncoding sequence and those of its somatic recombination partners, e.g., Ig C gamma 1, Ig C gamma 2b, Ig C alpha, because each of these 5' noncoding sequences is made of multiple copies in various stages of degeneracy of one primordial 20 base pair-long sequence: (AGCTG) (AGCTG) (AGCTG) (GGGTG).     

Disulfide bonds Cys(9)-Cys(57), Cys(34)-Cys(88) and Cys(38)-Cys(90) of the beta-subunit of human chorionic gonadotropin are crucial for heterodimer formation with the alpha-subunit: experimental evidence for the conclusions from the crystal structure of hCG

Human chorionic gonadotropin (hCG) is a heterodimeric glycoprotein hormone essential for the establishment and maintenance of pregnancy. The alpha- and beta-subunits of hCG are highly cross-linked internally by disulfide bonds that seem to stabilize the tertiary structures required for the noncovalent association of the subunits to generate hormonal activity. This paper describes the results of our studies on the role of the disulfide bonds of hCG-beta in heterodimer formation with the alpha-subunit. Six disulfide peptides incorporating each of the six disulfide bonds of hCG-beta were screened, along with their linear counterparts, for their ability to competitively inhibit the recombination of alpha- and beta-subunits. The disulfide peptides Cys (9-57), Cys (34-88) and Cys (38-90) were found to inhibit the alpha/beta recombination whereas the remaining three disulfide peptides viz. Cys (23-72), Cys (26-110) and Cys (93-100) did not exhibit any inhibition activity. Interestingly, none of the linear peptides could inhibit the alpha/beta recombination. Results clearly demonstrate that the disulfide bonds Cys(9)-Cys(57), Cys(34)-Cys(88) and Cys(38)-Cys(90) of the beta-subunit of hCG are crucial for heterodimer formation with the alpha-subunit thus providing experimental confirmation of the conclusions from the crystal structure of the hormone.     

铁线莲属研究随记(VI)(英文)

讨论了Clematis eriopoda Maxim.和sect.Atragenopsis Boiss.的地位,认为这二分类群均应成立;描述了2新种,1新变种;过去长期被归并的卷萼铁线莲C.tubulosa得到恢复;Clematisheracleifoliavar.ichangensis被转移改作卷萼铁线莲的变种;首次给出光叶铁线莲Clematisglabrifolia的果实的形态描述。     

The role of the CPNKEKEC sequence in the beta(2) subunit I domain in regulation of integrin alpha(L)beta(2) (LFA-1)

The alpha(L) I (inserted or interactive) domain of integrin alpha(L)beta(2) undergoes conformational changes upon activation. Recent studies show that the isolated, activated alpha(L) I domain is sufficient for strong ligand binding, suggesting the beta(2) subunit to be only indirectly involved. It has been unclear whether the activity of the alpha(L) I domain is regulated by the beta(2) subunit. In this study, we demonstrate that swapping the disulfide-linked CPNKEKEC sequence (residues 169-176) in the beta(2) I domain with a corresponding beta(3) sequence, or mutating Lys(174) to Thr, constitutively activates alpha(L)beta(2) binding to ICAM-1. These mutants do not require Mn(2+) for ICAM-1 binding and are insensitive to the inhibitory effect of Ca(2+). We have also localized a component of the mAb 24 epitope (a reporter of beta(2) integrin activation) in the CPNKEKEC sequence. Glu(173) and Glu(175) of the beta(2) I domain are identified as critical for mAb 24 binding. Because the epitope is highly expressed upon beta(2) integrin activation, it is likely that the CPNKEKEC sequence is exposed or undergoes conformational changes upon activation. Deletion of the alpha(L) I domain did not eliminate the mAb 24 epitope. This confirms that the alpha(L) I domain is not critical for mAb 24 binding, and indicates that mAb 24 detects a change expressed in part in the beta(2) subunit I domain. These results suggest that the CPNKEKEC sequence of the beta(2) I domain is involved in regulating the alpha(L) I domain.     

Improvement of efficiency of the Ce(IV)-induced DNA scission--relationship between the kinetic parameters (k(cat) and Km) and the DNA structure.

The Michaelis constant (Km) for double-stranded DNA, single-stranded DNA, and dinucleotide hydrolysis by Ce(IV) ion are 4.4, 15, and more than 40 mM, respectively. The order of the k(cat), however, is dinucleotide > oligonucleotides. Not only the improvement of k(cat) but also that of Km is important for the design of an efficient artificial nuclease.     

Comparison of the self-association properties of the 5'-triphosphates of inosine (ITP), guanosine (GTP), and adenosine (ATP). Further evidence for ionic interactions in the highly stable dimeric [H2(ATP)]2(4-) stack

The concentration dependence of the chemical shifts for the hydrogens H-2, H-8 and H-1' of ITP and for H-8 and H-1' of GTP has been measured in D2O at 25 degrees C under several degrees of protonation in the pD range 1.2-8.4. For reasons of comparison, inosine and guanosine have been included in the study The results are consistent with the isodesmic model of indefinite noncooperative stacking. The association constants for the nucleosides (Ns) inosine and guanosine decrease with increasing protonation: Ns greater than D(Ns)+/Ns in a 1:1 ratio greater than D(Ns)+. In contrast, a maximum is observed with ITP and GTP; the stacking tendency of GTP following the series: GTP4- less than or equal to D(GTP)3- (K approximately 0.7 M-1) less than D(GTP)3-/D2(GTP)2- in a 1:1 ratio (K approximately 2.9 M-1) greater than D2(GTP)2- greater than D3(GTP)- (K approximately 1.5 M-1). The order of the series with ITP corresponds to that with GTP, but the association constants are slightly smaller. At the maximum of the self-association tendency the triphosphate residue has only a minor influence; this follows from the fact that the association constants for the 1:1 ratios of Ino/D(Ino)+ and D(ITP)3-/D2(ITP)2- are identical within experimental error; this holds also for Guo/D(Guo)+ and D(GTP)3-/D2(GTP)2-; in all these pairs the K-7 site is 50% protonated. Comparison of the association constant for the deprotonated species shows that here charge effects, i.e. repulsion between the negatively charged triphosphate chains, are important: Ino (K approximately 3.3 M-1) greater than ITP4- (K approximately 0.4 M-1) and Guo (K approximately 8 M-1) greater than GTP4- (K approximately 0.8 M-1). In addition the series holds: Ado (K approximately 15 M-1) greater than Guo greater than Ino. However, most important is the comparison of the ITP and GTP series with previous data for ATP: ATP4- (K approximately 1.3 M-1) less than D(ATP)3- (2.1 M-1) less than 1:1 ratio of D(ATP)3-/D2(ATP)2- (6 M-1) much less than D2(ATP)2- (approximately 200 M-1) much greater than D3(ATP)- (K less than or equal to 17 M-1).(ABSTRACT TRUNCATED AT 400 WORDS)     

Oxydiacetato complexes of thorium(IV), the crystal structures of tetra-aquo bis(oxydiacetato)thorium(IV) hexahydrate and di(sodium nitrate) disodium tris(oxydiacetato)thorium(IV)

The crystal and molecular structures of Th(oda)₂(H₂O)₄·6H₂O (1) and Na₂[Th(oda)₃]·2NaNO₃ (2) (oda = oxydiacetate) have been determined from three-dimensional X-ray diffraction data and refined by least squares to R = 0.049 and Rw = 0.049 for 2265 independent reflections for (1) and to R = 0.024 and Rw = 0.023 for 2196 independent reflections for (2).Crystal parameters are as follows: (1), tetragonal, space group P4₁2₁2, a = 10.335(2), c = 20.709(5) Å and Z = 4; (2), monoclinic, space group C2/c, a = 17.096(5), b = 9.451(2), c = 16.245(4) Å, β = 107.8(1) and Z = 4.In both compounds the thorium atom lies on a crystallographic two-fold axis. The co-ordination number for thorium in (1) is 10 (bicapped square antiprism geometry), the compound is monomeric, the two oda ligands are tridentate to the metal, and four water molecules complete the coordination sphere; in thorium (2) the coordination number is 9 (tricapped trigonal prism geometry) with three oda ligands tridentate to the metal, the [Th(oda)₃]^2? and NO₃^? anions are held together through the sodium ions which are coordinated both to the oda carboxylic oxygens and to the nitrate oxygens.The ThO coordination distances are: in (1) 2.411(8), 2.414(9) for the carboxylic oxygens, 2.479(10) and 2.486(8) for water molecules and 2.697(9) for the etheric oxygen and in (2) 2.384(3), 2.402(4) and 2.402(4) for the carboxylic oxygens, 2.559(5) and 2.562(4) Å for the etheric oxygens.     

Mapping the collagen-binding site in the I domain of the glycoprotein Ia/IIa (integrin alpha(2)beta(1))

The I domain present within the alpha2 chain of the integrin alpha(2)beta(1) (GPIa/IIa) contains the principal collagen-binding site. Based on the crystal structure of the alpha2-I domain, a hypothetical model was proposed in which collagen binds to a groove on the upper surface of the I domain (Emsley, J., King, S. L., Bergelson, J. M., and Liddington, R. C. (1997) J. Biol. Chem. 272, 28512-28517). We have introduced point mutations into 13 residues on the upper surface of the domain. Recombinant mutant proteins were assayed for binding to monoclonal antibodies 6F1 and 12F1, to collagen under static conditions, and for the ability to retain adhesive activity under flow conditions. The mutations to residues surrounding the metal ion-dependent adhesion site that caused the greatest loss of collagen binding under both static and flow conditions are N154S in the betaA-alpha1 turn, N190D in the betaB-betaC turn, D219R in the alpha3-alpha4 turn, and E256V and H258V in the betaD-alpha5 turn. Mutation in one of the residues that coordinate the metal binding, S155A, completely lost the adhesive activity under flow but bound normally under static conditions, whereas the mutation Y285F had the converse effect. We conclude that the upper surface of the domain, including the metal ion-dependent adhesion site motif, defines the collagen recognition site.     

Linkage disequilibria and the site frequency spectra in the su(s) and su(w(a)) regions of the Drosophila melanogaster X chromosome

Over the last decade, surveys of DNA sequence variation in natural populations of several Drosophila species and other taxa have established that polymorphism is reduced in genomic regions characterized by low rates of crossing over per physical length. Parallel studies have also established that divergence between species is not reduced in these same genomic regions, thus eliminating explanations that rely on a correlation between the rates of mutation and crossing over. Several theoretical models (directional hitchhiking, background selection, and random environment) have been proposed as population genetic explanations. In this study samples from an African population (n = 50) and a European population (n = 51) were surveyed at the su(s) (1955 bp) and su(w(a)) (3213 bp) loci for DNA sequence polymorphism, utilizing a stratified SSCP/DNA sequencing protocol. These loci are located near the telomere of the X chromosome, in a region of reduced crossing over per physical length, and exhibit a significant reduction in DNA sequence polymorphism. Unlike most previously surveyed, these loci reveal substantial skews toward rare site frequencies, consistent with the predictions of directional hitchhiking and random environment models and inconsistent with the general predictions of the background selection model (or neutral theory). No evidence for excess geographic differentiation at these loci is observed. Although linkage disequilibrium is observed between closely linked sites within these loci, many recombination events in the genealogy of the sampled alleles can be inferred and the genomic scale of linkage disequilibrium, measured in base pairs between sites, is the same as that observed for loci in regions of normal crossing over. We conclude that gene conversion must be high in these regions of low crossing over.     

Bryozoan (Stenolaemata) records from the upper Callovian (Middle Jurassic) of the Moscow region

Encrusting bryozoans (Stenolaemata, Tubuliporida) discovered from upper Callovian deposits (Middle Jurassic) near the town of Kolomna in the Moscow region are described. They belong to two new species: Microeciella kolomnensis sp. nov. and Diplosolen akatjevense sp. nov. These bryozoans encrust a fragment of the large shell of cephalopod mollusk (ammonite), which is an unusual substrate not only for bryozoans but also for the other encrusting organisms.     

Energetics of the muricid gastropod Thais (Nucella) lapillus (L.)

Multivariate analysis of the physiological energetics of Thais (Nucella) lapillus (L.) was used to predict combinations of salinity and temperature at which scope for growth and reproduction will be positive. The scope for growth correlated positively with change in energy content at 15 and 20°C. The results suggest that energetic constraints set limits to capacity adaptation at ≈ 22‰ salinity, in agreement with field observations of the species distribution limit within estuaries. The zone of resistance adaptation is limited to salinities 15‰, probably because of an inefficiency in volume regulation at lower salinities. Growth of these dogwhelks is suppressed at minimum winter (5°C) and maximum summer (20°C) temperature, largely due to suppression of feeding. Constraints imposed by physiological energetics are important for an understanding of the ecology of this species, and may explain some features of seasonal change in behaviour, e.g. aggregations for purposes of egg-laying in the winter.     

Studies of the interaction of potassium(I), calcium(II), magnesium(II), and copper(II) with cyclosporin A

Metal ion binding properties of the immunosuppressant drug cyclosporin A have been investigated. Complexation studies in acetonitrile solution using 1H NMR and CD spectroscopy yielded 1:1 metal-peptide binding constants (log(10)K) for potassium(I), <1, magnesium(II), 4.8+/-0.2, and calcium(II), 5.0+/-1.0. The interaction of copper(II) with cyclosporin A in methanol was investigated with UV/visible and electron paramagnetic resonance (EPR) spectroscopy. No complexation of copper(II) was observed in neutral solution. In the presence of base, monomeric copper(II) complexes were detected. These results support the possibility that cyclosporin A has ionophoric properties for biologically important essential metal ions.     

Functional coupling of the beta(1) subunit to the large conductance Ca(2+)-activated K(+) channel in the absence of Ca(2+). Increased Ca(2+) sensitivity from a Ca(2+)-independent mechanism

Coexpression of the beta(1) subunit with the alpha subunit (mSlo) of BK channels increases the apparent Ca(2+) sensitivity of the channel. This study investigates whether the mechanism underlying the increased Ca(2+) sensitivity requires Ca(2+), by comparing the gating in 0 Ca(2+)(i) of BK channels composed of alpha subunits to those composed of alpha+beta(1) subunits. The beta(1) subunit increased burst duration approximately 20-fold and the duration of gaps between bursts approximately 3-fold, giving an approximately 10-fold increase in open probability (P(o)) in 0 Ca(2+)(i). The effect of the beta(1) subunit on increasing burst duration was little changed over a wide range of P(o) achieved by varying either Ca(2+)(i) or depolarization. The effect of the beta(1) subunit on increasing the durations of the gaps between bursts in 0 Ca(2+)(i) was preserved over a range of voltage, but was switched off as Ca(2+)(i) was increased into the activation range. The Ca(2+)-independent, beta(1) subunit-induced increase in burst duration accounted for 80% of the leftward shift in the P(o) vs. Ca(2+)(i) curve that reflects the increased Ca(2+) sensitivity induced by the beta(1) subunit. The Ca(2+)-dependent effect of the beta(1) subunit on the gaps between bursts accounted for the remaining 20% of the leftward shift. Our observation that the major effects of the beta(1) subunit are independent of Ca(2+)(i) suggests that the beta(1) subunit mainly alters the energy barriers of Ca(2+)-independent transitions. The changes in gating induced by the beta(1) subunit differ from those induced by depolarization, as increasing P(o) by depolarization or by the beta(1) subunit gave different gating kinetics. The complex gating kinetics for both alpha and alpha+beta(1) channels in 0 Ca(2+)(i) arise from transitions among two to three open and three to five closed states and are inconsistent with Monod-Wyman-Changeux type models, which predict gating among only one open and one closed state in 0 Ca(2+)(i).