Altering coenzyme specificity of xylose reductase by the semi-rational approach CASTing-0

<p><b>Copyright information:</b></p><p>Taken from "Altering coenzyme specificity of xylose reductase by the semi-rational approach CASTing"</p><p>http://www.microbialcellfactories.com/content/6/1/36</p><p>Microbial Cell Factories 2007;6():36-36.</p><p>Published online 21 Nov 2007</p><p>PMCID:PMC2213684.</p><p></p>TG (1 mM). Crude extracts of different variants were adjusted to the same ODconcentration (12.41 OD/ml) before they were prepared, and 15 μl was loaded in each lane. Lanes: 1, the insoluble fraction of NT-XR; 2, the soluble fraction of NT-XR; 3, the insoluble fraction of pET30a; 4, the soluble fraction of pET30a; 5, marker; 6, the insoluble fraction of XR; 7, the soluble fraction of XR; 8, the soluble fraction of CT-XR; 9, the insoluble fraction of CT-XR

Altering coenzyme specificity of xylose reductase by the semi-rational approach CASTing-2

<p><b>Copyright information:</b></p><p>Taken from "Altering coenzyme specificity of xylose reductase by the semi-rational approach CASTing"</p><p>http://www.microbialcellfactories.com/content/6/1/36</p><p>Microbial Cell Factories 2007;6():36-36.</p><p>Published online 21 Nov 2007</p><p>PMCID:PMC2213684.</p><p></p>inding sites of wild-type NT-XR with NADPH. NADPH was in purple. The figures were prepared with VMD 1.8.4 [30], based on a structural model for PsXR obtained via homology modeling using the TASSER-Lite [15, 16, 31]. Red, green and blue colors indicate rounds 1, 2, 3 residues, respectively

Altering coenzyme specificity of xylose reductase by the semi-rational approach CASTing-3

<p><b>Copyright information:</b></p><p>Taken from "Altering coenzyme specificity of xylose reductase by the semi-rational approach CASTing"</p><p>http://www.microbialcellfactories.com/content/6/1/36</p><p>Microbial Cell Factories 2007;6():36-36.</p><p>Published online 21 Nov 2007</p><p>PMCID:PMC2213684.</p><p></p>TG (1 mM). Crude extracts of different variants were adjusted to the same ODconcentration (12.41 OD/ml) before they were prepared, and 15 μl was loaded in each lane. Lanes: 1, the insoluble fraction of NT-XR; 2, the soluble fraction of NT-XR; 3, the insoluble fraction of pET30a; 4, the soluble fraction of pET30a; 5, marker; 6, the insoluble fraction of XR; 7, the soluble fraction of XR; 8, the soluble fraction of CT-XR; 9, the insoluble fraction of CT-XR

Altering coenzyme specificity of xylose reductase by the semi-rational approach CASTing-1

<p><b>Copyright information:</b></p><p>Taken from "Altering coenzyme specificity of xylose reductase by the semi-rational approach CASTing"</p><p>http://www.microbialcellfactories.com/content/6/1/36</p><p>Microbial Cell Factories 2007;6():36-36.</p><p>Published online 21 Nov 2007</p><p>PMCID:PMC2213684.</p><p></p>[8]. And the residues predicted to be involved in coenzyme binding in PsXR are exactly the same as the corresponding CtXR residues (indicated in brackets). The corresponding CtXR residues are indicated in brackets

Charge Transfer Structure–Reactivity Dependence of Fullerene–Single-Walled Carbon Nanotube Heterojunctions

Charge transfer at the interface between single-walled carbon nanotubes (SWCNTs) of distinct chiral vectors and fullerenes of various molecular weights is of interest both fundamentally and because of its importance in emerging photovoltaic and optoelectronic devices. One approach for generating isolated, discretized fullerene–SWCNT heterojunctions for spectroscopic investigation is to form an amphiphile, which is able to disperse the latter at the single-SWCNT level in aqueous solution. Herein, we synthesize a series of methanofullerene amphiphiles, including derivatives of C₆₀, C₇₀, and C₈₄, and investigated their electron transfer with SWCNT of specific chirality, generating a structure–reactivity relationship. In the cases of two fullerene derivatives, lipid–C₆₁–polyethylene glycol (PEG) and lipid–C₇₁–PEG, band gap dependent, incomplete quenching was observed across all SWCNT species, indicating that the driving force for electron transfer is small. This is further supported by a variant of Marcus theory, which predicts that the energy offsets between the nanotube conduction bands and the C₆₁ and C₇₁ LUMO levels are less than the exciton binding energy in SWCNT. In contrast, upon interfacing nanotubes with C₈₅ methanofullerene, a complete quenching of all semiconducting SWCNT is observed. This enhancement in quenching efficiency is consistent with the deeper LUMO level of C₈₅ methanofullerene in comparison with the smaller fullerene adducts, and suggests its promise as for SWCNT–fullerene heterojunctions

2D Equation-of-State Model for Corona Phase Molecular Recognition on Single-Walled Carbon Nanotube and Graphene Surfaces

Corona phase molecular recognition (CoPhMoRe) has been recently introduced as a means of generating synthetic molecular recognition sites on nanoparticle surfaces. A synthetic heteropolymer is adsorbed and confined to the surface of a nanoparticle, forming a corona phase capable of highly selective molecular recognition due to the conformational imposition of the particle surface on the polymer. In this work, we develop a computationally predictive model for analytes adsorbing onto one type of polymer corona phase composed of hydrophobic anchors on hydrophilic loops around a single-walled carbon nanotube (SWCNT) surface using a 2D equation of state that takes into consideration the analyte−polymer, analyte−nanoparticle, and polymer−nanoparticle interactions using parameters determined independently from molecular simulation. The SWCNT curvature is found to contribute weakly to the overall interaction energy, exhibiting no correlation for three of the corona phases considered, and differences of less than 5% and 20% over a larger curvature range for two other corona phases, respectively. Overall, the resulting model for this anchor-loop CoPhMoRe is able to correctly predict 83% of an experimental 374 analyte–polymer library, generating experimental fluorescence responses within 20% error of the experimental values. The modeling framework presented here represents an important step forward in the design of suitable polymers to target specific analytes

Effects of evodiamine (EVO) on the protein expression of Cyt C, caspase-12, -8, -9 and -3, Fas and Trail in the H446 and H1688 SCLC cells.

<p>Cell lysates were analyzed by Western blot. Each experiment was repeated 3 times. Data presented as mean ± standard deviation (n = 3). Untreated H446 or H1688 cells were used as a negative control group. *<i>P</i><0.05 as compared to corresponding control group. Fas: factor associated suicide; Trail: tumor necrosis factor-related apoptosis inducing ligand; Cyt C: cytochrome C.</p

Effects of evodiamine (EVO) on the cell cycle distribution and apoptosis rate of the H446 and H1688 SCLC cells.

<p>Cell cycle was detected by PI assay. Apoptosis was detected using an Annexin V/PI double staining assay. The H446 cells stained with Annexin V/PI were observed under an inverted fluorescence microscope. Each experiment was repeated 3 times. Data presented as mean ± standard deviation (n = 3). *<i>P</i><0.05 as compared to corresponding control group. Untreated H446 or H1688 cells were used as a negative control group.</p

Effects of evodiamine (EVO) on the mRNA expression of Bax and Bcl-2 in H446 and H1688 cells.

<p>Cell lysates were analyzed by RT-PCR. Each experiment was repeated 3 times. Data presented as mean ± standard deviation (n = 3). Untreated H446 or H1688 cells were used as a negative control group. *<i>P</i><0.05 as compared to the control group. ^#<i>P</i><0.05 as compared to corresponding EVO treated group at 24 h. <i>P</i><0.05 as compared to corresponding EVO treated group at 48 h.</p

Evodiamine (EVO) induces apoptosis through two intrinsic caspase-dependent pathways, but not through an extrinsic caspase-dependent pathway.

<p>Evodiamine (EVO) induces apoptosis through two intrinsic caspase-dependent pathways, but not through an extrinsic caspase-dependent pathway.</p