2 research outputs found
Flexible Silver Nanowire Meshes for High-Efficiency Microtextured Organic-Silicon Hybrid Photovoltaics
Hybrid organic-silicon heterojunction solar cells promise
a significant reduction on fabrication costs by avoiding energy-intensive
processes. However, their scalability remains challenging without
a low-cost transparent electrode. In this work, we present solution-processed
silver-nanowire meshes that uniformly cover the microtextured surface
of hybrid heterojunction solar cells to enable efficient carrier collection
for large device area. We systematically compare the characteristics
and device performance with long and short nanowires with an average
length/diameter of 30 μm/115 nm and 15 μm/45 nm, respectively,
to those with silver metal grids. A remarkable power conversion efficiency
of 10.1% is achieved with a device area of 1 × 1 cm<sup>2</sup> under 100 mW/cm<sup>2</sup> of AM1.5G illumination for the hybrid
solar cells employing long wires, which represents an enhancement
factor of up to 36.5% compared to the metal grid counterpart. The
high-quality nanowire network displays an excellent spatial uniformity
of photocurrent generation via distributed nanowire meshes and low
dependence on efficient charge transport under a high light-injection
condition with increased device area. The capability of silver nanowires
as flexible transparent electrodes presents a great opportunity to
accelerate the mass deployment of high-efficiency hybrid silicon photovoltaics
via simple and rapid soluble processes
High-Throughput Screening of Sulfated Proteins by Using a Genome-Wide Proteome Microarray and Protein Tyrosine Sulfation System
Protein
tyrosine sulfation (PTS) is a widespread posttranslational
modification that induces intercellular and extracellular responses
by regulating protein–protein interactions and enzymatic activity.
Although PTS affects numerous physiological and pathological processes,
only a small fraction of the total predicted sulfated proteins has
been identified to date. Here, we localized the potential sulfation
sites of Escherichia coli proteins
on a proteome microarray by using a 3′-phosphoadenosine 5′-phosphosulfate
(PAPS) synthase-coupled tyrosylprotein sulfotransferase (TPST) catalysis
system that involves in situ PAPS generation and TPST catalysis. Among
the 4256 E. coli K12 proteins, 875
sulfated proteins were identified using antisulfotyrosine primary
and Cy3-labeled antimouse secondary antibodies. Our findings add considerably
to the list of potential proteins subjected to tyrosine sulfation.
Similar procedures can be applied to identify sulfated proteins in
yeast and human proteome microarrays, and we expect such approaches
to contribute substantially to the understanding of important human
diseases