9 research outputs found
Kinetic Evaluation of Cyclopentane as a Promoter for CO<sub>2</sub> Capture via a Clathrate Process Employing Different Contact Modes
In
order to mitigate global warming with growing demands on fossil
fuels, it is essential to reduce CO<sub>2</sub> emissions from the
energy sector. Hydrate-based CO<sub>2</sub> capture from fuel gas
mixture (40% CO<sub>2</sub>/60% H<sub>2</sub>) is one of the options
to reduce the carbon footprint of power plants. This work employed
cyclopentane (CP) as a promoter and investigated the kinetic performance
of CP/CO<sub>2</sub>/H<sub>2</sub> hydrate formation with two different
contact modes using an unstirred tank reactor (UTR) and a fixed bed
reactor (FBR) at 281.2 K and 6.0 MPa. Repeat cycles were conducted
to examine the recyclability of reactants. Compared with UTR,
FBR showed a higher hydrate formation rate and improved the gas uptake
by enhancing the dissolution phase. A distinctive two-stage hydrate
growth was observed in UTR. Morphology observations were coupled with
kinetic data to present the characteristic growth behavior of CP/CO<sub>2</sub>/H<sub>2</sub> hydrate. Furthermore, the scalability of the
hydrate formation process was examined. A FBR approach employing a
tray column design (three trays) was developed to scale up the bed
size without sacrificing the overall kinetics. Lastly, the effect
of vacuum on gas recovery from hydrate dissociation was studied, and
a CO<sub>2</sub> composition enrichment as high as 97.9% was achieved.
Overall, the high gas uptake and high CO<sub>2</sub> content enriched
show the advantages of employing FBR for CP/CO<sub>2</sub>/H<sub>2</sub> hydrate formation. However, one major challenge to be addressed
is to avoid the loss of CP between repeat cycles caused by its volatile
nature
Table1_Service scheduling strategy for microservice and heterogeneous multi-cores-based edge computing apparatus in smart girds with high renewable energy penetration.DOCX
The microservice-based smart grid service (SGS) organization and the heterogeneous multi-cores-based computing resource supply are the development direction of edge computing in smart grid with high penetration of renewable energy sources and high market-oriented. However, their application also challenges the service schedule for edge computing apparatus (ECA), the physical carrier of edge computing. In the traditional scheduling strategy of SGS, an SGS usually corresponds to an independent application or component, and the heterogeneous multi-core computing environment is also not considered, making it difficult to cope with the above challenges. In this paper, we propose an SGS scheduling strategy for the ECA. Specifically, we first present an SGS scheduling framework of ECA and give the essential element of meeting SGS scheduling. Then, considering the deadline and importance attributes of the SGS, a microservice scheduling prioritizing module is proposed. On this basis, the inset-based method is used to allocate the microservice task to the heterogeneous multi-cores to utilize computing resources and reduce the service response time efficiently. Furthermore, we design the scheduling unit dividing module to balance the delay requirement between the service with early arrival time and the service with high importance in high concurrency scenarios. An emergency mechanism (EM) is also presented for the timely completion of urgent SGSs. Finally, the effectiveness of the proposed service scheduling strategy is verified in a typical SGS scenario in the smart distribution transformer area.</p
Highly Efficient and Reversible SO<sub>2</sub> Capture by Surfactant-Derived Dual Functionalized Ionic Liquids with Metal Chelate Cations
A series
of dual functionalized ionic liquids with metal chelate
cations from surfactant and alkali metal salt were designed, prepared,
and used for SO<sub>2</sub> capture. The effect of metal ions, coordination
number, anionic structures, temperature, and pressure on SO<sub>2</sub> absorption was investigated. The interaction of these functionalized
ionic liquids with SO<sub>2</sub> was explained by spectroscopic investigation.
The results showed that these metal-containing ionic liquids exhibited
high absorption capacity through a combination of physical and chemical
interaction of SO<sub>2</sub> with basic anions and ether-containing
cations as well as excellent reversibility (21 recycles). Considering
the easy preparation, low cost, and excellent performance, these dual
functionalized metal-containing ionic liquids provide significant
improvements over traditional ionic liquids, indicating the promise
for industrial application in SO<sub>2</sub> capture
Additional file 1 of Prediction of the efficacy of group cognitive behavioral therapy using heart rate variability based smart wearable devices: a randomized controlled study
Supplementary Material
Systematic Analysis of Missing Proteins Provides Clues to Help Define All of the Protein-Coding Genes on Human Chromosome 1
Our
first proteomic exploration of human chromosome 1 began in
2012 (CCPD 1.0), and the genome-wide characterization of the human
proteome through public resources revealed that 32–39% of proteins
on chromosome 1 remain unidentified. To characterize all of the missing
proteins, we applied an OMICS-integrated analysis of three human liver
cell lines (Hep3B, MHCC97H, and HCCLM3) using mRNA and ribosome nascent-chain
complex-bound mRNA deep sequencing and proteome profiling, contributing
mass spectrometric evidence of 60 additional chromosome 1 gene products.
Integration of the annotation information from public databases revealed
that 84.6% of genes on chromosome 1 had high-confidence protein evidence.
Hierarchical analysis demonstrated that the remaining 320 missing
genes were either experimentally or biologically explainable; 128
genes were found to be tissue-specific or rarely expressed in some
tissues, whereas 91 proteins were uncharacterized mainly due to database
annotation diversity, 89 were genes with low mRNA abundance or unsuitable
protein properties, and 12 genes were identifiable theoretically because
of a high abundance of mRNAs/RNC-mRNAs and the existence of proteotypic
peptides. The relatively large contribution made by the identification
of enriched transcription factors suggested specific enrichment of
low-abundance protein classes, and SRM/MRM could capture high-priority
missing proteins. Detailed analyses of the differentially expressed
genes indicated that several gene families located on chromosome 1
may play critical roles in mediating hepatocellular carcinoma invasion
and metastasis. All mass spectrometry proteomics data corresponding
to our study were deposited in the ProteomeXchange under the identifiers
PXD000529, PXD000533, and PXD000535
Systematic Analysis of Missing Proteins Provides Clues to Help Define All of the Protein-Coding Genes on Human Chromosome 1
Our
first proteomic exploration of human chromosome 1 began in
2012 (CCPD 1.0), and the genome-wide characterization of the human
proteome through public resources revealed that 32–39% of proteins
on chromosome 1 remain unidentified. To characterize all of the missing
proteins, we applied an OMICS-integrated analysis of three human liver
cell lines (Hep3B, MHCC97H, and HCCLM3) using mRNA and ribosome nascent-chain
complex-bound mRNA deep sequencing and proteome profiling, contributing
mass spectrometric evidence of 60 additional chromosome 1 gene products.
Integration of the annotation information from public databases revealed
that 84.6% of genes on chromosome 1 had high-confidence protein evidence.
Hierarchical analysis demonstrated that the remaining 320 missing
genes were either experimentally or biologically explainable; 128
genes were found to be tissue-specific or rarely expressed in some
tissues, whereas 91 proteins were uncharacterized mainly due to database
annotation diversity, 89 were genes with low mRNA abundance or unsuitable
protein properties, and 12 genes were identifiable theoretically because
of a high abundance of mRNAs/RNC-mRNAs and the existence of proteotypic
peptides. The relatively large contribution made by the identification
of enriched transcription factors suggested specific enrichment of
low-abundance protein classes, and SRM/MRM could capture high-priority
missing proteins. Detailed analyses of the differentially expressed
genes indicated that several gene families located on chromosome 1
may play critical roles in mediating hepatocellular carcinoma invasion
and metastasis. All mass spectrometry proteomics data corresponding
to our study were deposited in the ProteomeXchange under the identifiers
PXD000529, PXD000533, and PXD000535
Systematic Analysis of Missing Proteins Provides Clues to Help Define All of the Protein-Coding Genes on Human Chromosome 1
Our
first proteomic exploration of human chromosome 1 began in
2012 (CCPD 1.0), and the genome-wide characterization of the human
proteome through public resources revealed that 32–39% of proteins
on chromosome 1 remain unidentified. To characterize all of the missing
proteins, we applied an OMICS-integrated analysis of three human liver
cell lines (Hep3B, MHCC97H, and HCCLM3) using mRNA and ribosome nascent-chain
complex-bound mRNA deep sequencing and proteome profiling, contributing
mass spectrometric evidence of 60 additional chromosome 1 gene products.
Integration of the annotation information from public databases revealed
that 84.6% of genes on chromosome 1 had high-confidence protein evidence.
Hierarchical analysis demonstrated that the remaining 320 missing
genes were either experimentally or biologically explainable; 128
genes were found to be tissue-specific or rarely expressed in some
tissues, whereas 91 proteins were uncharacterized mainly due to database
annotation diversity, 89 were genes with low mRNA abundance or unsuitable
protein properties, and 12 genes were identifiable theoretically because
of a high abundance of mRNAs/RNC-mRNAs and the existence of proteotypic
peptides. The relatively large contribution made by the identification
of enriched transcription factors suggested specific enrichment of
low-abundance protein classes, and SRM/MRM could capture high-priority
missing proteins. Detailed analyses of the differentially expressed
genes indicated that several gene families located on chromosome 1
may play critical roles in mediating hepatocellular carcinoma invasion
and metastasis. All mass spectrometry proteomics data corresponding
to our study were deposited in the ProteomeXchange under the identifiers
PXD000529, PXD000533, and PXD000535
Systematic Analysis of Missing Proteins Provides Clues to Help Define All of the Protein-Coding Genes on Human Chromosome 1
Our
first proteomic exploration of human chromosome 1 began in
2012 (CCPD 1.0), and the genome-wide characterization of the human
proteome through public resources revealed that 32–39% of proteins
on chromosome 1 remain unidentified. To characterize all of the missing
proteins, we applied an OMICS-integrated analysis of three human liver
cell lines (Hep3B, MHCC97H, and HCCLM3) using mRNA and ribosome nascent-chain
complex-bound mRNA deep sequencing and proteome profiling, contributing
mass spectrometric evidence of 60 additional chromosome 1 gene products.
Integration of the annotation information from public databases revealed
that 84.6% of genes on chromosome 1 had high-confidence protein evidence.
Hierarchical analysis demonstrated that the remaining 320 missing
genes were either experimentally or biologically explainable; 128
genes were found to be tissue-specific or rarely expressed in some
tissues, whereas 91 proteins were uncharacterized mainly due to database
annotation diversity, 89 were genes with low mRNA abundance or unsuitable
protein properties, and 12 genes were identifiable theoretically because
of a high abundance of mRNAs/RNC-mRNAs and the existence of proteotypic
peptides. The relatively large contribution made by the identification
of enriched transcription factors suggested specific enrichment of
low-abundance protein classes, and SRM/MRM could capture high-priority
missing proteins. Detailed analyses of the differentially expressed
genes indicated that several gene families located on chromosome 1
may play critical roles in mediating hepatocellular carcinoma invasion
and metastasis. All mass spectrometry proteomics data corresponding
to our study were deposited in the ProteomeXchange under the identifiers
PXD000529, PXD000533, and PXD000535
Systematic Analysis of Missing Proteins Provides Clues to Help Define All of the Protein-Coding Genes on Human Chromosome 1
Our
first proteomic exploration of human chromosome 1 began in
2012 (CCPD 1.0), and the genome-wide characterization of the human
proteome through public resources revealed that 32–39% of proteins
on chromosome 1 remain unidentified. To characterize all of the missing
proteins, we applied an OMICS-integrated analysis of three human liver
cell lines (Hep3B, MHCC97H, and HCCLM3) using mRNA and ribosome nascent-chain
complex-bound mRNA deep sequencing and proteome profiling, contributing
mass spectrometric evidence of 60 additional chromosome 1 gene products.
Integration of the annotation information from public databases revealed
that 84.6% of genes on chromosome 1 had high-confidence protein evidence.
Hierarchical analysis demonstrated that the remaining 320 missing
genes were either experimentally or biologically explainable; 128
genes were found to be tissue-specific or rarely expressed in some
tissues, whereas 91 proteins were uncharacterized mainly due to database
annotation diversity, 89 were genes with low mRNA abundance or unsuitable
protein properties, and 12 genes were identifiable theoretically because
of a high abundance of mRNAs/RNC-mRNAs and the existence of proteotypic
peptides. The relatively large contribution made by the identification
of enriched transcription factors suggested specific enrichment of
low-abundance protein classes, and SRM/MRM could capture high-priority
missing proteins. Detailed analyses of the differentially expressed
genes indicated that several gene families located on chromosome 1
may play critical roles in mediating hepatocellular carcinoma invasion
and metastasis. All mass spectrometry proteomics data corresponding
to our study were deposited in the ProteomeXchange under the identifiers
PXD000529, PXD000533, and PXD000535