Assessment of Colorimetric Reporter Enzymes in the PURE System.

Colorimetric reporter enzymes are useful for generating eye-readable biosensor readouts that do not require a device to interpret, an attractive property for applications in remote or developing parts of the world. The use of cell-free gene expression further facilitates such applications amenability to lyophilization and incorporation into materials like paper. Currently, detection of multiple analytes simultaneously with these systems requires multiple reactions or a device.

Rapid Characterization of Genetic Parts with Cell-free Systems.

Characterizing and cataloging genetic parts are critical to the design of useful genetic circuits. Having well-characterized parts allows for the fine-tuning of genetic circuits, such that their function results in predictable outcomes. With the growth of synthetic biology as a field, there has been an explosion of genetic circuits that have been implemented in microbes to execute functions pertaining to sensing, metabolic alteration, and cellular computing.

Synthesis and characterisation of thin-film platinum disulfide and platinum sulfide.

Group-10 transition metal dichalcogenides (TMDs) are rising in prominence within the highly innovative field of 2D materials. While PtS has been investigated for potential electronic applications, due to its high charge-carrier mobility and strongly layer-dependent bandgap, it has proven to be one of the more difficult TMDs to synthesise. In contrast to most TMDs, Pt has a significantly more stable monosulfide, the non-layered PtS.

Low-temperature synthesis and electrocatalytic application of large-area PtTe thin films.

The synthesis of transition metal dichalcogenides (TMDs) has been a primary focus for 2D nanomaterial research over the last 10 years, however, only a small fraction of this research has been concentrated on transition metal ditellurides. In particular, nanoscale platinum ditelluride (PtTe) has rarely been investigated, despite its potential applications in catalysis, photonics and spintronics. Of the reports published, the majority examine mechanically-exfoliated flakes from chemical vapor transport (CVT) grown crystals.

A method for cost-effective and rapid characterization of engineered T7-based transcription factors by cell-free protein synthesis reveals insights into the regulation of T7 RNA polymerase-driven expression.

The T7 bacteriophage RNA polymerase (T7 RNAP) serves as a model for understanding RNA synthesis, as a tool for protein expression, and as an actuator for synthetic gene circuit design in bacterial cells and cell-free extract. T7 RNAP is an attractive tool for orthogonal protein expression in bacteria owing to its compact single subunit structure and orthogonal promoter specificity. Understanding the mechanisms underlying T7 RNAP regulation is important to the design of engineered T7-based transcription factors, which can be used in gene circuit design.

Ultrafast Carrier Dynamics and Bandgap Renormalization in Layered PtSe.

Carrier interactions in 2D nanostructures are of central importance not only in condensed-matter physics but also for a wide range of optoelectronic and photonic applications. Here, new insights into the behavior of photoinduced carriers in layered platinum diselenide (PtSe ) through ultrafast time-resolved pump-probe and nonlinear optical measurements are presented. The measurements reveal the temporal evolution of carrier relaxation, chemical potential and bandgap renormalization in PtSe .

Convergent evolution of hetero-oligomeric cellulose synthesis complexes in mosses and seed plants.

In seed plants, cellulose is synthesized by rosette-shaped cellulose synthesis complexes (CSCs) that are obligate hetero-oligomeric, comprising three non-interchangeable cellulose synthase (CESA) isoforms. The moss Physcomitrella patens has rosette CSCs and seven CESAs, but its common ancestor with seed plants had rosette CSCs and a single CESA gene. Therefore, if P.

Kinetic analysis of cellulose synthase of Gluconacetobacter hansenii in whole cells and in purified form.

The Gram-negative bacterium, Gluconacetobacter hansenii, has been long studied and is a model for cellulose synthesis. It produces cellulose, using the enzyme AcsA-AcsB, of exceptionally high crystallinity in comparison to the cellulose of higher plants. We determined the rate of cellulose synthesis in whole cells measured as moles of glucose incorporated into cellulose per second per mole of enzyme.

Initiation, Elongation, and Termination of Bacterial Cellulose Synthesis.

Cellulose is the major component of the plant cell wall and composed of β-linked glucose units. Use of cellulose is greatly impacted by its physical properties, which are dominated by the number of individual cellulose strand within each fiber and the average length of each strand. Our work described herein provides a complete mechanism for cellulose synthase accounting for its processivity and mechanism of initiation.

A New 2H-2H'/1T Cophase in Polycrystalline MoS and MoSe Thin Films.

We report on 2H-2H'/1T phase conversion of MoS and MoSe polycrystalline films grown by thermally assisted conversion. The structural conversion of the transition metal dichalcogenides was successfully carried out by organolithium treatment on chip. As a result we obtained a new 2H-2H'/1T cophase system of the TMDs thin films which was verified by Raman spectroscopy, X-ray diffraction, and X-ray photoelectron spectroscopy.

AcsA-AcsB: The core of the cellulose synthase complex from Gluconacetobacter hansenii ATCC23769.

The gram-negative bacterium, Gluconacetobacter hansenii, produces cellulose of exceptionally high crystallinity in comparison to the cellulose of higher plants. This bacterial cellulose is synthesized and extruded into the extracellular medium by the cellulose synthase complex (CSC). The catalytic component of this complex is encoded by the gene AcsAB.

Processing of cellulose synthase (AcsAB) from Gluconacetobacter hansenii 23769.

The cellulose synthase protein (AcsAB) is encoded by a single gene in Gluconacetobacter hansenii ATCC 23769. We have examined the processing pattern of this enzyme and the localization of the cleavage products by heterologously expressing the truncated portions of the AcsAB protein and using specific antibodies generated against these regions. We found that the AcsAB protein is processed into three polypeptide subunits of molecular masses 46kDa, 34kDa and 95kDa.