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Hydrophobic Surface (hydrophobic + surface)
Selected AbstractsExpression Profile During the Development of Appressoria Induced by Hydrophobic Surfaces in Magnaporthe grisea Y34JOURNAL OF PHYTOPATHOLOGY, Issue 3 2010Qingchao Jin Abstract To study the gene expression profile during appressorium developmental process of Magnaphorthe grisea strain Y34 isolated from the rich area of Asia cultivated rice resources, expressed sequence tags (ESTs) and cDNA array analysis were performed. A total of 4756 tentative unique transcripts (TUTs) were obtained from 13 057 ESTs of the 3, ends of the strain, which was approximately 25% of the total M. grisea EST sequences deposited in the GenBank database. Approximately 84% of these TUTs matched with the published draft genome sequences of strain 70-15. Southern analyses with 12 TUT probes revealed no obvious DNA polymorphism among strains 70-15, Guy11 and Y34. A cDNA array with 4108 TUTs was used to monitor gene expression patterns during appressorium development of M. grisea. Compared with ungerminated conidia, the number of up-regulated and down-regulated genes was almost consistent at any time-points of 2, 8, 20 and 30 h during appressorium development. More genes were differentially expressed during appressorium maturation (20 and 30 h) than during appressorium induction (2 h) and formation (8 h). During appressorium maturation (20,30 h), genes generally seemed to be most actively expressed. [source] Microchannels Constructed on Rough Hydrophobic SurfacesCHEMICAL ENGINEERING & TECHNOLOGY (CET), Issue 8 2008M. Watanabe Abstract A microchannel was constructed between two glass slides, taking advantage of their surface properties. The channel geometry was defined by a line that was previously printed on the slide surface using a highly water-soluble liquid [2-(2-ethoxyethoxy)ethanol] as the ink. Water, which acted as the working fluid flowed along this line. Although the channel did not have any sidewalls, the water was fixed along the printed line due to the large contact-angle hysteresis of the slide surface whose properties were rough and hydrophobic. Such roughness was more advantageous over smoothness due to the large contact-angle hysteresis of water and the good wettability of the ink. Using a syringe pump, the water was able to continuously flow through a 1,mm wide and 0.13,mm deep channel without flooding. [source] Solution structure of the bb, domains of human protein disulfide isomeraseFEBS JOURNAL, Issue 5 2009Alexey Y. Denisov Protein disulfide isomerase is the most abundant and best studied of the disulfide isomerases that catalyze disulfide bond formation in the endoplasmic reticulum, yet the specifics of how it binds substrate have been elusive. Protein disulfide isomerase is composed of four thioredoxin-like domains (abb,a,). Cross-linking studies with radiolabeled peptides and unfolded proteins have shown that it binds incompletely folded proteins primarily via its third domain, b,. Here, we determined the solution structure of the second and third domains of human protein disulfide isomerase (b and b,, respectively) by triple-resonance NMR spectroscopy and molecular modeling. NMR titrations identified a large hydrophobic surface within the b, domain that binds unfolded ribonuclease A and the peptides mastoparan and somatostatin. Protein disulfide isomerase-catalyzed refolding of reduced ribonuclease A in vitro was inhibited by these peptides at concentrations equal to their affinity to the bb, fragment. Our findings provide a structural basis for previous kinetic and cross-linking studies which have shown that protein disulfide isomerase exhibits a saturable, substrate-binding site. [source] Organic Electronics: High Tg Cyclic Olefin Copolymer Gate Dielectrics for N,N,-Ditridecyl Perylene Diimide Based Field-Effect Transistors: Improving Performance and Stability with Thermal Treatment (Adv. Funct.ADVANCED FUNCTIONAL MATERIALS, Issue 16 2010Mater. Abstract A novel application of ethylene-norbornene cyclic olefin copolymers (COC) as gate dielectric layers in organic field-effect transistors (OFETs) that require thermal annealing as a strategy for improving the OFET performance and stability is reported. The thermally-treated N,N, -ditridecyl perylene diimide (PTCDI-C13)-based n-type FETs using a COC/SiO2 gate dielectric show remarkably enhanced atmospheric performance and stability. The COC gate dielectric layer displays a hydrophobic surface (water contact angle = 95° ± 1°) and high thermal stability (glass transition temperature = 181 °C) without producing crosslinking. After thermal annealing, the crystallinity improves and the grain size of PTCDI-C13 domains grown on the COC/SiO2 gate dielectric increases significantly. The resulting n-type FETs exhibit high atmospheric field-effect mobilities, up to 0.90 cm2 V,1 s,1 in the 20 V saturation regime and long-term stability with respect to H2O/O2 degradation, hysteresis, or sweep-stress over 110 days. By integrating the n-type FETs with p-type pentacene-based FETs in a single device, high performance organic complementary inverters that exhibit high gain (exceeding 45 in ambient air) are realized. [source] High Tg Cyclic Olefin Copolymer Gate Dielectrics for N,N,-Ditridecyl Perylene Diimide Based Field-Effect Transistors: Improving Performance and Stability with Thermal TreatmentADVANCED FUNCTIONAL MATERIALS, Issue 16 2010Jaeyoung Jang Abstract A novel application of ethylene-norbornene cyclic olefin copolymers (COC) as gate dielectric layers in organic field-effect transistors (OFETs) that require thermal annealing as a strategy for improving the OFET performance and stability is reported. The thermally-treated N,N, -ditridecyl perylene diimide (PTCDI-C13)-based n-type FETs using a COC/SiO2 gate dielectric show remarkably enhanced atmospheric performance and stability. The COC gate dielectric layer displays a hydrophobic surface (water contact angle = 95° ± 1°) and high thermal stability (glass transition temperature = 181 °C) without producing crosslinking. After thermal annealing, the crystallinity improves and the grain size of PTCDI-C13 domains grown on the COC/SiO2 gate dielectric increases significantly. The resulting n-type FETs exhibit high atmospheric field-effect mobilities, up to 0.90 cm2 V,1 s,1 in the 20 V saturation regime and long-term stability with respect to H2O/O2 degradation, hysteresis, or sweep-stress over 110 days. By integrating the n-type FETs with p-type pentacene-based FETs in a single device, high performance organic complementary inverters that exhibit high gain (exceeding 45 in ambient air) are realized. [source] Surface-Modified High- k Oxide Gate Dielectrics for Low-Voltage High-Performance Pentacene Thin-Film Transistors,ADVANCED FUNCTIONAL MATERIALS, Issue 6 2007S. Kim Abstract In this study, pentacene thin-film transistors (TFTs) operating at low voltages with high mobilities and low leakage currents are successfully fabricated by the surface modification of the CeO2,SiO2 gate dielectrics. The surface of the gate dielectric plays a crucial role in determining the performance and electrical reliability of the pentacene TFTs. Nearly hysteresis-free transistors are obtained by passivating the devices with appropriate polymeric dielectrics. After coating with poly(4-vinylphenol) (PVP), the reduced roughness of the surface induces the formation of uniform and large pentacene grains; moreover, ,OH groups on CeO2,SiO2 are terminated by C6H5, resulting in the formation of a more hydrophobic surface. Enhanced pentacene quality and reduced hysteresis is observed in current,voltage (I,V) measurements of the PVP-coated pentacene TFTs. Since grain boundaries and ,OH groups are believed to act as electron traps, an OH-free and smooth gate dielectric leads to a low trap density at the interface between the pentacene and the gate dielectric. The realization of electrically stable devices that can be operated at low voltages makes the OTFTs excellent candidates for future flexible displays and electronics applications. [source] High-Field Scanning Probe Lithography in Hexadecane: Transitioning from Field Induced Oxidation to Solvent Decomposition through Surface Modification,ADVANCED MATERIALS, Issue 21 2007I. Suez High field scanning probe lithography in hexadecane leads to two different chemical reactions depending on surface hydrophilicity. On a hydrophilic surface, oxidation of the sample occurs; a hydrophobic surface, results in solvent decomposition and nanoscale deposition of etch resistant material. The features are characterized with photoelectron emission microscopy and are carbonaceous in nature with a highly cross-linked bonding network. Tone reversal in a fluorinated etch is achieved. [source] HTPB-based polyurethaneurea membranes for recovery of aroma compounds from aqueous solution by pervaporationJOURNAL OF APPLIED POLYMER SCIENCE, Issue 1 2007Yunxiang Bai Abstract Hydroxyterminated polybutadiene (HTPB)-based polyurethaneurea (PU), HTPB-PU, was synthesized by two-step polymerization and was firstly used as membrane materials to recover aroma, ethyl acetate (EA), from aqueous solution by pervaporation (PV). The effects of the number,average molecular weight (Mn) of HTPB, EA in feed, operating temperature, and membrane thickness on the PV performance of HTPB-PU membranes were investigated. The membranes demonstrated high EA permselectivity as well as high EA flux. The DSC result showed two transition temperatures in the HTPB-PU membrane and contact angle measurements revealed the difference of hydrophobicity of the membrane at both sides, which were induced by glass plate and air, respectively, due to movement of the soft hydrophobic polybutadiene (PB) segments in HTPB-PU chains. Furthermore, the PV performance of the HTPB-PU membrane with the hydrophobic surface facing the feed was much better than that with the hydrophilic surface. © 2007 Wiley Periodicals, Inc. J Appl Polym Sci 104: 552,559, 2007 [source] Fusion core structure of the severe acute respiratory syndrome coronavirus (SARS-CoV): In search of potent SARS-CoV entry inhibitorsJOURNAL OF CELLULAR BIOCHEMISTRY, Issue 6 2008Ling-Hon Matthew Chu Abstract Severe acute respiratory coronavirus (SARS-CoV) spike (S) glycoprotein fusion core consists of a six-helix bundle with the three C-terminal heptad repeat (HR2) helices packed against a central coiled-coil of the other three N-terminal heptad repeat (HR1) helices. Each of the three peripheral HR2 helices shows prominent contacts with the hydrophobic surface of the central HR1 coiled-coil. The concerted protein,protein interactions among the HR helices are responsible for the fusion event that leads to the release of the SARS-CoV nucleocapsid into the target host-cell. In this investigation, we applied recombinant protein and synthetic peptide-based biophysical assays to characterize the biological activities of the HR helices. In a parallel experiment, we employed a HIV-luc/SARS pseudotyped virus entry inhibition assay to screen for potent inhibitory activities on HR peptides derived from the SARS-CoV S protein HR regions and a series of other small-molecule drugs. Three HR peptides and five small-molecule drugs were identified as potential inhibitors. ADS-J1, which has been used to interfere with the fusogenesis of HIV-1 onto CD4+ cells, demonstrated the highest HIV-luc/SARS pseudotyped virus-entry inhibition activity among the other small-molecule drugs. Molecular modeling analysis suggested that ADS-J1 may bind to the deep pocket of the hydrophobic groove on the surface of the central coiled-coil of SARS-CoV S HR protein and prevent the entrance of the SARS-CoV into the host cells. J. Cell. Biochem. 104: 2335,2347, 2008. © 2008 Wiley-Liss, Inc. [source] Behavioral patterns of drop impingement onto rigid substrates with a wide range of wettability and different surface temperaturesAICHE JOURNAL, Issue 8 2009Xiying Li Abstract This article concerns behavioral patterns of droplet impingement onto solid substrates covering a wide range of wettability from hydrophilic to superhydrophobic surfaces heated at different temperatures. For droplet impingement onto partial hydrophobic surfaces (mirror-polished Cu substrate), the maximum heights of receding droplet undergoing a consecutive increment with surface temperature can be explained taking account of Marangoni flow. Also, the relation to predict the increment of droplet heights with surface temperature was manifested in the light of lubrication approximation combined with energy conservation. However, this relation is only valid for droplet impacts onto partial hydrophobic surface, because the recoiling droplet height was observed to be independent of surface temperature for both hydrophilic and superhydrophobic targets. This phenomenon was attributed to inherent wettability accompanying larger contact angle hysteresis for the hydrophilic substrate and to the presence of an adiabatic gas layer between the composite surface and impacting droplet, for the superhydrophobic target. © 2009 American Institute of Chemical Engineers AIChE J, 2009 [source] Orexin-A is composed of a highly conserved C -terminal and a specific, hydrophilic N -terminal region, revealing the structural basis of specific recognition by the orexin-1 receptorJOURNAL OF PEPTIDE SCIENCE, Issue 7 2006Tomoyo Takai Abstract Orexins-A and B, also called hypocretins-1 and 2, respectively, are neuropeptides that regulate feeding and sleep-wakefulness by binding to two orphan G protein-coupled receptors named orexin-1 (OX1R) and orexin-2 (OX2R). The sequences and functions of orexins-A and B are similar to each other, but the high sequence homology (68%) is limited in their C -terminal half regions (residues 15,33). The sequence of the N -terminal half region of orexin-A (residues 1,14), containing two disulfide bonds, is very different from that of orexin-B. The structure of orexin-A was determined using two-dimensional homonuclear and 15N and 13C natural abundance heteronuclear NMR experiments. Orexin-A had a compact conformation in the N -terminal half region, which contained a short helix (III:Cys6-Gln9) and was fixed by the two disulfide bonds, and a helix-turn-helix conformation (I:Leu16-Ala23 and II:Asn25-Thr32) in the remaining C -terminal half region. The C -terminal half region had both hydrophobic and hydrophilic residues, which existed on separate surfaces to provide an amphipathic character in helices I and II. The nine residues on the hydrophobic surface are also well conserved in orexin-B, and it was reported that the substitution of each of them with alanine resulted in a significant drop in the functional potency at the receptors. Therefore, we suggest that they form the surface responsible for the main hydrophobic interaction with the receptors. On the other hand, the residues on the hydrophilic surface, together with the hydrophilic residues in the N -terminal half region that form a cluster, are known to make only small contributions to the binding to the receptors through similar alanine-scan experiments. However, since our structure of orexin-A showed that large conformational and electrostatical differences between orexins-A and B were rather concentrated in the N -terminal half regions, we suggest that the region of orexin-A is important for the preference for orexin-A of OX1R. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd. [source] Osteoblast Adhesion and Proliferation on Poly(3-octylthiophene) Thin FilmsMACROMOLECULAR BIOSCIENCE, Issue 3 2010Charlene Rincón Abstract In this study we assessed the suitability of semiconducting P3OT thin films (30,nm) to sustain attachment, spreading, and proliferation of MC3T3-E1 osteoblasts. Cell area correlated with surface wettability: area was larger on the more hydrophilic surface (TCPS) and lower on the more hydrophobic surface (P3OT). Cells were rounder, characterized by higher circularity values, on TCPS and Si compared to P3OT. P3OT proliferation rate at 24,h fell twofold after 48,h, then recovered at 72,h to a value significantly higher than that on TCPS. Presoaking experiments showed no evidence of cytotoxic effects or leachants from P3OT. Overall, we conclude that P3OT is a viable substrate for osteoblast attachment and proliferation. [source] Functional regions of the N-terminal domain of the antiterminator RfaHMOLECULAR MICROBIOLOGY, Issue 2 2010Georgiy A. Belogurov Summary RfaH is a bacterial elongation factor that increases expression of distal genes in several long, horizontally acquired operons. RfaH is recruited to the transcription complex during RNA chain elongation through specific interactions with a DNA element called ops. Following recruitment, RfaH remains bound to RNA polymerase (RNAP) and acts as an antiterminator by reducing RNAP pausing and termination at some factor-independent and Rho-dependent signals. RfaH consists of two domains connected by a flexible linker. The N-terminal RfaH domain (RfaHN) recognizes the ops element, binds to the RNAP and reduces pausing and termination in vitro. Functional analysis of single substitutions in this domain reported here suggests that three separate RfaHN regions mediate these functions. We propose that a polar patch on one side of RfaHN interacts with the non-template DNA strand during recruitment, whereas a hydrophobic surface on the opposite side of RfaHN remains bound to the ,, subunit clamp helices domain throughout transcription of the entire operon. The third region is apparently dispensable for RfaH binding to the transcription complex but is required for the antitermination modification of RNAP. [source] Removing the invariant salt bridge of parvalbumin increases flexibility in the AB -loop structureACTA CRYSTALLOGRAPHICA SECTION D, Issue 8 2009François Hoh Parvalbumins (PVs) are calcium-buffer proteins that belong to the EF-hand family. Their N-terminal domain consists of two antiparallel helices A and B that make up a flat hydrophobic surface that is associated with the opposite side of the CD and EF binding sites. A single conserved Arg75,Glu81 salt bridge is buried in this hydrophobic interface. The structure of a rat PV mutant in which Arg75 was replaced by alanine was solved by molecular replacement. Unexpectedly, a large distance deviation of 7.8,Å was observed for the AB loop but not for the residues that flank the R75A mutation. The thermal stability of the calcium-loaded form is lower (Tm = 352.0,K; ,Tm = ,11.4,K) than that of the wild-type protein and the apo mutant is unfolded at room temperature. Weaker calcium or magnesium affinities were also measured for the R75A mutant (Ca2+: K1 = 4.21 × 107,M,1, K2 = 6.18 × 106,M,1; Mg2+: K1 = 2.98 × 104,M,1, K2 = 3.09 × 103,M,1). Finally, comparison of the B factors showed an increase in the flexibility of the AB loop that is consistent with this region being more exposed to solvent in the mutant. The mutant structure therefore demonstrates the role of the salt bridge in attaching the nonbinding AB domain to the remaining protein core. Normal-mode analysis indeed indicated an altered orientation of the AB domain with regard to the CD,EF binding domains. [source] A charged residue at the subunit interface of PCNA promotes trimer formation by destabilizing alternate subunit interactionsACTA CRYSTALLOGRAPHICA SECTION D, Issue 6 2009Bret D. Freudenthal Eukaryotic proliferating cell nuclear antigen (PCNA) is an essential replication accessory factor that interacts with a variety of proteins involved in DNA replication and repair. Each monomer of PCNA has an N-terminal domain A and a C-terminal domain B. In the structure of the wild-type PCNA protein, domain A of one monomer interacts with domain B of a neighboring monomer to form a ring-shaped trimer. Glu113 is a conserved residue at the subunit interface in domain A. Two distinct X-ray crystal structures have been determined of a mutant form of PCNA with a substitution at this position (E113G) that has previously been studied because of its effect on translesion synthesis. The first structure was the expected ring-shaped trimer. The second structure was an unanticipated nontrimeric form of the protein. In this nontrimeric form, domain A of one PCNA monomer interacts with domain A of a neighboring monomer, while domain B of this monomer interacts with domain B of a different neighboring monomer. The B,B interface is stabilized by an antiparallel ,-sheet and appears to be structurally similar to the A,B interface observed in the trimeric form of PCNA. The A,A interface, in contrast, is primarily stabilized by hydrophobic interactions. Because the E113G substitution is located on this hydrophobic surface, the A,A interface should be less favorable in the case of the wild-type protein. This suggests that the side chain of Glu113 promotes trimer formation by destabilizing these possible alternate subunit interactions. [source] The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfacesACTA CRYSTALLOGRAPHICA SECTION D, Issue 5 2009Inge Van Molle Many Gram-negative bacteria use the chaperone,usher pathway to express adhesive surface structures, such as fimbriae, in order to mediate attachment to host cells. Periplasmic chaperones are required to shuttle fimbrial subunits or pilins through the periplasmic space in an assembly-competent form. The chaperones cap the hydrophobic surface of the pilins through a donor-strand complementation mechanism. FaeE is the periplasmic chaperone required for the assembly of the F4 fimbriae of enterotoxigenic Escherichia coli. The FaeE crystal structure shows a dimer formed by interaction between the pilin-binding interfaces of the two monomers. Dimerization and tetramerization have been observed previously in crystal structures of fimbrial chaperones and have been suggested to serve as a self-capping mechanism that protects the pilin-interactive surfaces in solution in the absence of the pilins. However, thermodynamic and biochemical data show that FaeE occurs as a stable monomer in solution. Other lines of evidence indicate that self-capping of the pilin-interactive interfaces is not a mechanism that is conservedly applied by all periplasmic chaperones, but is rather a case-specific solution to cap aggregation-prone surfaces. [source] Structure of a new crystal form of tetraubiquitinACTA CRYSTALLOGRAPHICA SECTION D, Issue 2 2001Cynthia L. Phillips Polyubiquitin chains, in which the C-terminus and a lysine side chain of successive ubiquitin molecules are linked by an isopeptide bond, function to target substrate proteins for degradation by the 26S proteasome. Chains of at least four ubiquitin moieties appear to be required for efficient recognition by the 26S proteasome, although the conformations of the polyubiquitin chains recognized by the proteasome or by other enzymes involved in ubiquitin metabolism are currently unknown. A new crystal form of tetraubiquitin, which has two possible chain connectivities that are indistinguishable in the crystal, is reported. In one possible connectivity, the tetraubiquitin chain is extended and packs closely against the antiparallel neighbor chain in the crystal to conceal a hydrophobic surface implicated in 26S proteasome recognition. In the second possibility, the tetraubiqutitin forms a closed compact structure, in which that same hydrophobic surface is buried. Both of these conformations are quite unlike the structure of tetraubiquitin that was previously determined in a different crystal form [Cook et al. (1994), J. Mol. Biol.236, 601,609]. The new structure suggests that polyubiquitin chains may possess a substantially greater degree of conformational flexibility than has previously been appreciated. [source] Contact Angle, WAXS, and SAXS Analysis of Poly(,-hydroxybutyrate) and Poly(ethylene glycol) Block Copolymers Obtained via Azotobacter vinelandii UWDBIOTECHNOLOGY PROGRESS, Issue 3 2005Kerry J. Townsend This study investigated and correlated physical properties and cell interactions of copolymers obtained by a poly(ethylene glycol) (PEG)-modulated fermentation of Azotobacter vinelandii UWD. PEGs with molecular weights of 400 and 3400 Da and di(ethylene glycol) (DEG) were used to modulate the bacterial synthesis of poly(,-hydroxybutyrate) (PHB). The PHB crystallinity was determined by wide-angle X-ray scattering (WAXS). Small-angle X-ray scattering (SAXS) showed that lamellar distances decreased between the PHB and the PHB modulated with PEG or DEG. Furthermore, the contact angle of water on the PHB/PEG polymer surfaces decreased when compared to that of PHB. The significant decrease of the contact angle and corresponding increase in surface tension, as well as significant decrease in cell adhesion, suggest the presence of hydrophilic PEG and DEG within the hydrophobic surface. [source] Studies on the conformational properties of CP-1042,55, the hinge region of CP-10, using circular dichroism and RP-HPLCCHEMICAL BIOLOGY & DRUG DESIGN, Issue 6 2000E. Lazoura Abstract: The conformational properties of CP-1042,55, a peptide corresponding to the hinge region of CP-10, were investigated using circular dichroism spectroscopy and reverse-phase high-performance liquid chromatography (RP-HPLC). The circular dichroism studies indicated that CP-1042,55 formed considerable secondary structure in the presence of hydrophobic solution environments including 50% acetonitrile, 50% trifluoroethanol and 200 mm sodium dodecyl sulfate, which comprised a mixture of ,-helix and ,-sheet. The effect of temperature on the conformation of CP-1042,55 was investigated between 5 and 40°C, with very small changes in the spectra being observed.RP-HPLC was then used to investigate the effect of temperature on the conformation of CP-1042,55 in the presence of a hydrophobic surface. Using a C18 -adsorbent, CP-1042,55 exhibited a conformational transition at 25°C, which was associated with an increase in the chromatographic contact area and the binding affinity of the peptide for the stationary phase. In addition, near-planar bandbroadening behaviour indicated that conformational species interconverted with rapid rate constants compared with the chromatographic time scale. These results indicated that the conformational change at 25°C in theRP-HPLC system most likely corresponds to the unfolding of an ,-helical and/or ,-sheet structure to an extended coil structure. Therefore, the strong chemotactic properties of this peptide may be attributed to its ability to form considerable secondary structure in the presence of a hydrophobic environment. [source] Periodic Mesoporous Organosilicas: A Type of Hybrid Support for Water-Mediated ReactionsCHEMISTRY - AN ASIAN JOURNAL, Issue 7 2007Ying Wan Prof. Abstract Hybrid mesoporous periodic organosilicas (Ph-PMOs) with phenylene moieties embedded inside the silica matrix were used as a heterogeneous catalyst for the Ullmann coupling reaction in water. XRD, N2 sorption, TEM, and solid-state NMR spectroscopy reveal that mesoporous Ph-PMO supports and Pd/Ph-PMO catalysts have highly ordered 2D hexagonal mesostructures and covalently bonded organic,inorganic (all Si atoms bonded with carbon) hybrid frameworks. In the Ullmann coupling reaction of iodobenzene in water, the yield of biphenyl was 94,%, 34,%, 74,% and for palladium-supported Ph-PMO, pure silica (MCM-41), and phenyl-group-modified Ph-MCM-41 catalysts, respectively. The selectivity toward biphenyl reached 91,% for the coupling of boromobenzene on the Pd/Ph-PMO catalyst. This value is much higher than that for Pd/Ph-MCM-41 (19,%) and Pd/MCM-41 (0,%), although the conversion of bromobenzene for these two catalysts is similar to that for Pd/Ph-PMO. The large difference in selectivity can be attributed to surface hydrophobicity, which was evaluated by the adsorption isotherms of water and toluene. Ph-PMO has the most hydrophobic surface, and in turn selectively adsorbs the reactant haloaryls from aqueous solution. Water transfer inside the mesochannels is thus restricted, and the coupling reaction of bromobenzene is improved. [source] Glycosylation Enhances Peptide Hydrophobic Collapse by Impairing SolvationCHEMPHYSCHEM, Issue 11 2010Shanmei Cheng Dr. Abstract Post-translational N-glycosylation of proteins is ubiquitous in eukaryotic cells, and has been shown to influence the thermodynamics of protein collapse and folding. However, the mechanism for this influence is not well understood. All-atom molecular dynamics simulations are carried out to study the collapse of a peptide linked to a single N-glycan. The glycan is shown to perturb the local water hydrogen-bonding network, rendering it less able to solvate the peptide and thus enhancing the hydrophobic contribution to the free energy of collapse. The enhancement of the hydrophobic collapse compensates for the weakened entropic coiling due to the bulky glycan chain and leads to a stronger burial of hydrophobic surface, presumably enhancing folding. This conclusion is reinforced by comparison with coarse-grained simulations, which contain no explicit solvent and correspondingly exhibit no significant thermodynamic changes on glycosylation. [source] The Influence of Surface Chemistry and Pore Size on the Adsorption of Proteins on Nanostructured Carbon MaterialsADVANCED FUNCTIONAL MATERIALS, Issue 15 2010Munusami Vijayaraj Abstract Carbon films are synthesized by templating of anodic aluminum oxide films. These carbon materials exhibit nanochannels with controlled diameter and length. Selected chemical treatments are done to tailor the surface chemistry. The adsorption capacities of bovine serum albumin and cytochrome c are measured by temperature-programmed desorption with mass spectrometry (TPD-MS) analysis and with conventional biological assays. The first method allows quantification of the proteins that exhibit strong interactions with the surface, while the second one is used to obtain the total adsorption capacity. Moreover, the TPD-MS profiles, which are related to the structural modifications of the proteins during the adsorption, show that strong interactions take place with hydrophobic surfaces. When oxygenated functions are present, the adsorption capacity increases and the nature of the interactions is modified. The ratio of irreversible to reversible adsorption is significantly different for the two proteins, and is slightly related to the surface chemistry. The influence of nanochannel size is studied: below 50 nm, the coverage ratio shows that access to the porosity is limited by diffusion in the channel and by pore plugging, in agreement with the strong interactions of proteins with the carbon surface. [source] Self-Assembly of DNA-Templated Polypyrrole Nanowires: Spontaneous Formation of Conductive Nanoropes,ADVANCED FUNCTIONAL MATERIALS, Issue 16 2008Stela Pruneanu Abstract Polypyrrole nanowires formed by polymerization of pyrrole on a DNA template self-assemble into rope-like structures. These ,nanoropes' may be quite smooth (diameters 5,30,nm) or may show frayed ends where individual strands are visible. A combination of electric force microscopy, conductive atomic force microscopy and two-terminal current,voltage measurements show that they are conductive. Nanoropes adhere more weakly to hydrophobic surfaces prepared by silanization of SiO2 than to the clean oxide; this effect can be used to aid the combing of the nanoropes across microelectrode devices for electrical characterization. [source] Behavioral patterns of drop impingement onto rigid substrates with a wide range of wettability and different surface temperaturesAICHE JOURNAL, Issue 8 2009Xiying Li Abstract This article concerns behavioral patterns of droplet impingement onto solid substrates covering a wide range of wettability from hydrophilic to superhydrophobic surfaces heated at different temperatures. For droplet impingement onto partial hydrophobic surfaces (mirror-polished Cu substrate), the maximum heights of receding droplet undergoing a consecutive increment with surface temperature can be explained taking account of Marangoni flow. Also, the relation to predict the increment of droplet heights with surface temperature was manifested in the light of lubrication approximation combined with energy conservation. However, this relation is only valid for droplet impacts onto partial hydrophobic surface, because the recoiling droplet height was observed to be independent of surface temperature for both hydrophilic and superhydrophobic targets. This phenomenon was attributed to inherent wettability accompanying larger contact angle hysteresis for the hydrophilic substrate and to the presence of an adiabatic gas layer between the composite surface and impacting droplet, for the superhydrophobic target. © 2009 American Institute of Chemical Engineers AIChE J, 2009 [source] Stabilization mechanisms of organic matter in four temperate soils: Development and application of a conceptual model,JOURNAL OF PLANT NUTRITION AND SOIL SCIENCE, Issue 1 2008Margit von Lützow Abstract Based on recent findings in the literature, we developed a process-oriented conceptual model that integrates all three process groups of organic matter (OM) stabilization in soils namely (1) selective preservation of recalcitrant compounds, (2) spatial inaccessibility to decomposer organisms, and (3) interactions of OM with minerals and metal ions. The model concept relates the diverse stabilization mechanisms to active, intermediate, and passive pools. The formation of the passive pool is regarded as hierarchical structured co-action of various processes that are active under specific pedogenetic conditions. To evaluate the model, we used data of pool sizes and turnover times of soil OM fractions from horizons of two acid forest and two agricultural soils. Selective preservation of recalcitrant compounds is relevant in the active pool and particularly in soil horizons with high C contents. Biogenic aggregation preserves OM in the intermediate pool and is limited to topsoil horizons. Spatial inaccessibility due to the occlusion of OM in clay microstructures and due to the formation of hydrophobic surfaces stabilizes OM in the passive pool. If present, charcoal contributes to the passive pool mainly in topsoil horizons. The importance of organo-mineral interactions for OM stabilization in the passive pool is well-known and increases with soil depth. Hydrophobicity is particularly relevant in acid soils and in soils with considerable inputs of charcoal. We conclude that the stabilization potentials of soils are site- and horizon-specific. Furthermore, management affects key stabilization mechanisms. Tillage increases the importance of organo-mineral interactions for OM stabilization, and in Ap horizons with high microbial activity and C turnover, organo-mineral interactions can contribute to OM stabilization in the intermediate pool. The application of our model showed that we need a better understanding of processes causing spatial inaccessibility of OM to decomposers in the passive pool. [source] Determination of the secondary structure of proteins in different environments by FTIR-ATR spectroscopy and PLS regressionBIOPOLYMERS, Issue 11 2008Yeqiu Wang Abstract The secondary structures of proteins (,-helical, ,-sheet, ,-turn, and random coil) in the solid state and when bound to polymer beads, containing immobilized phenyl and butyl ligands such as those as commonly employed in hydrophobic interaction chromatography, have been investigated using FTIR-ATR spectroscopy and partial least squares (PLS) methods. Proteins with known structural features were used as models, including 12 proteins in the solid state and 7 proteins adsorbed onto the hydrophobic surfaces. A strong PLS correlation was achieved between predictions derived from the experimental data for 4 proteins adsorbed onto the phenyl-modified beads and reference data obtained from the X-ray crystallographic structures with r2 values of 0.9974, 0.9864, 0.9924, and 0.9743 for ,-helical, ,-sheet, ,-turn, and random coiled structures, respectively. On the other hand, proteins adsorbed onto the butyl sorbent underwent greater secondary structural changes compared to the phenyl sorbent as evidenced from the poorer PLS r2 values (r2 are 0.9658, 0.9106, 0.9571, and 0.9340). The results thus indicate that the secondary structures for these proteins were more affected by the butyl sorbent, whereas the secondary structure remains relatively unchanged for the proteins adsorbed onto the phenyl sorbent. This study has important ramifications for understanding the nature of protein secondary structural changes following adsorption onto hydrophobic sorbent surfaces. This knowledge could also enable the development of useful protocols for enhancing the chromatographic purification of proteins in their native bioactive states. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 895,905, 2008. This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com [source] ,-sheet folding of 11-kDa fibrillogenic polypeptide is completely aggregation drivenBIOPOLYMERS, Issue 4 2007Natalya I. Topilina Abstract A de novo polypeptide GH6[(GA)3GY(GA)3GE]8GAH6 (YE8) was designed and genetically engineered to form antiparallel ,-strands of GAGAGA repeats. Modulation of pH enables control of solubility, folding, and aggregation of YE8 by control of the overall polypeptide charge, a consequence of the protonation or deprotonation of the glutamic acid and histidine residues. YE8 exhibits all the major properties of a fibrillogenic protein providing an excellent model for detailed study of the fibrillation. At neutral pH, YE8 is soluble in disordered form, yet at pH 3.5 folds into a predominantly ,-sheet conformation that is fibrillogenic. Atomic force microscopy and transmission electron microscopy indicated the formation of fibrillar aggregates on well-defined, hydrophobic surfaces. The ,-sheet folding of YE8 exhibited a lag phase that could be eliminated by seeding or stirring. The strong dependence of lag time on polypeptide concentration established the limiting step in aggregation as initiation of ,-sheet folding. © 2007 Wiley Periodicals, Inc. Biopolymers 86: 261,264, 2007. This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com [source] Refolding of proteins from inclusion bodies is favored by a diminished hydrophobic effect at elevated pressuresBIOTECHNOLOGY & BIOENGINEERING, Issue 2 2009Ryan L. Crisman Abstract The application of high hydrostatic pressure is an effective tool to promote dissolution and refolding of protein from aggregates and inclusion bodies while minimizing reaggregation. In this study we explored the mechanism of high-pressure protein refolding by quantitatively assessing the magnitude of the protein,protein interactions both at atmospheric and elevated pressures for T4 lysozyme, in solutions containing various amounts of guanidinium hydrochloride. At atmospheric pressure, the protein, protein interactions are most attractive at moderate guanidinium hydrochloride concentrations (,1,2 molar), as indicated by a minimum in B22 values. In contrast, at a pressure of 1,000 bar no minimum in B22 values is observed, indicating that high pressures colloidally stabilize protein against aggregation. Finally, experimental values of refractive index increments as a function of pressure indicate that at high pressures, wetting of the hydrophobic surfaces is favored, resulting in a reduction of the hydrophobic effect. This reduction in the hydrophobic effect reduces the driving force for aggregation of (partially) unfolded protein. Biotechnol. Bioeng. 2009;102: 483,492. © 2008 Wiley Periodicals, Inc. [source] Efficient and scalable method for scaling up cell free protein synthesis in batch modeBIOTECHNOLOGY & BIOENGINEERING, Issue 4 2005Alexei M. Voloshin A novel method for general cell free system scale-up in batch mode was applied to expression of E. coli chloramphenicol acetyl transferase (CAT) and a GMCSF-scFv fusion protein being developed as a B-cell lymphoma vaccine candidate (GLH). Performance of two different E. coli based cell-free systems was evaluated using the new scale-up approach. Reaction volumes from 15 to 500 µL were tested for both products and both reaction systems. In each case, the new scale-up method preserved total, soluble, and active volumetric yields of GLH and CAT at every reaction volume. At the 500 µL reaction volume, the PANOx SP system produced 560,±,36 µg/mL of active CAT and 99,±,10 µg/mL of active GLH protein using the new thin film approach whereas 500 µL test tube reactions produced 250,±,42 µg/mL and 72,±,7 µg/mL of active CAT and GLH respectively. Similarly, 500 µL cell-free synthesis reactions with the Cytomim system produced 481,±,38 µg/mL of active CAT and 109,±,15 µg/mL active GLH respectively in thin films compared to 29,±,7 µg/mL of active CAT and 5,±,2 µg/mL of active GLH protein in 500 µL test tube reactions. The new thin film approach improves oxygen supply for the Cytomim system, and increases the availability of hydrophobic surfaces. Analysis suggests that these surfaces provide significant benefit for protein expression and folding. We believe that this approach provides a general reaction scale-up technology that will be suitable for any protein target, cell free system, and reaction volume. © 2005 Wiley Periodicals, Inc. [source] | ||||||||||||||||