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  • 1
    Publication Date: 2016-04-17
    Description: We report the crystal structure and hole-transport mechanism in spiro-OMeTAD [2,2',7,7'-tetrakis( N , N -di- p -methoxyphenyl-amine)9,9'-spirobifluorene], the dominant hole-transporting material in perovskite and solid-state dye-sensitized solar cells. Despite spiro-OMeTAD’s paramount role in such devices, its crystal structure was unknown because of highly disordered solution-processed films; the hole-transport pathways remained ill-defined and the charge carrier mobilities were low, posing a major bottleneck for advancing cell efficiencies. We devised an antisolvent crystallization strategy to grow single crystals of spiro-OMeTAD, which allowed us to experimentally elucidate its molecular packing and transport properties. Electronic structure calculations enabled us to map spiro-OMeTAD’s intermolecular charge-hopping pathways. Promisingly, single-crystal mobilities were found to exceed their thin-film counterparts by three orders of magnitude. Our findings underscore mesoscale ordering as a key strategy to achieving breakthroughs in hole-transport material engineering of solar cells.
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
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  • 2
    Publication Date: 2017-07-22
    Description: High energy and safe electrochemical storage are critical components in multiple emerging fields of technologies. Rechargeable lithium-metal batteries are considered to be promising alternatives for current lithium-ion batteries, leading to as much as a 10-fold improvement in anode storage capacity (from 372 to 3860 mAh g –1 ). One of the major challenges for commercializing lithium-metal batteries is the reliability and safety issue, which is often associated with uneven lithium electrodeposition (lithium dendrites) during the charging stage of the battery cycling process. We report that stable lithium-metal batteries can be achieved by simply charging cells with square-wave pulse current. We investigated the effects of charging period and frequency as well as the mechanisms that govern this process at the molecular level. Molecular simulations were performed to study the diffusion and the solvation structure of lithium cations (Li + ) in bulk electrolyte. The model predicts that loose association between cations and anions can enhance the transport of Li + and eventually stabilize the lithium electrodeposition. We also performed galvanostatic measurements to evaluate the cycling behavior and cell lifetime under pulsed electric field and found that the cell lifetime can be more than doubled using certain pulse current waveforms. Both experimental and simulation results demonstrate that the effectiveness of pulse current charging on dendrite suppression can be optimized by choosing proper time- and frequency-dependent pulses. This work provides a molecular basis for understanding the mechanisms of pulse current charging to mitigating lithium dendrites and designing pulse current waveforms for stable lithium-metal batteries.
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
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  • 3
    Publication Date: 2019
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 2019
    Description: 〈p〉Reducing human reliance on energy-inefficient cooling methods such as air conditioning would have a large impact on the global energy landscape. By a process of complete delignification and densification of wood, we developed a structural material with a mechanical strength of 404.3 megapascals, more than eight times that of natural wood. The cellulose nanofibers in our engineered material backscatter solar radiation and emit strongly in mid-infrared wavelengths, resulting in continuous subambient cooling during both day and night. We model the potential impact of our cooling wood and find energy savings between 20 and 60%, which is most pronounced in hot and dry climates.〈/p〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2019
    Description: 〈p〉The recently discovered topological phase offers new possibilities for spintronics and condensed matter. Even insulating material exhibits conductivity at the edges of certain systems, giving rise to an anomalous quantum Hall effect and other coherent spin transport phenomena, in which heat dissipation is minimized, with potential uses for next-generation energy-efficient electronics. While the metallic surface states of topological insulators (TIs) have been extensively studied, direct comparison of the surface and bulk magnetic properties of TIs has been little explored. We report unambiguous evidence for distinctly enhanced surface magnetism in a prototype magnetic TI, Cr-doped Bi〈sub〉2〈/sub〉Se〈sub〉3〈/sub〉. Using synchrotron-based x-ray techniques, we demonstrate a "three-step transition" model, with a temperature window of ~15 K, where the TI surface is magnetically ordered while the bulk is not. Understanding the dual magnetization process has strong implications for defining a physical model of magnetic TIs and lays the foundation for applications to information technology.〈/p〉
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
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  • 6
    Publication Date: 2001-12-26
    Description: Bacterial surface appendages called pili and needle-like filaments are associated with protein and/or DNA transfer to recipient plant, human, or bacterial cells during pathogenesis or conjugation. Although it has long been suspected that pili function as a conduit for protein or DNA transfer, direct evidence has been lacking. The Hrp pilus of Pseudomonas syringae is assembled by the type III secretion system. We used an in situ immunogold labeling procedure to visualize the extrusion of an effector protein, AvrPto, from the tip of the Hrp pilus, providing direct evidence that a bacterial pilus can function as a conduit for protein delivery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jin, Q -- He, S Y -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2556-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Energy Plant Research Laboratory and Department of Plant Biology, Michigan State University, East Lansing, MI 48824, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11752577" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Bacterial ; Bacterial Proteins/analysis/genetics/immunology/*metabolism ; DEAD-box RNA Helicases ; *Escherichia coli Proteins ; Fimbriae, Bacterial/chemistry/*metabolism/ultrastructure ; Immunohistochemistry ; Microscopy, Immunoelectron ; Polysaccharide-Lyases/analysis/immunology ; Pseudomonas/genetics/*metabolism/ultrastructure ; *RNA Helicases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 2001-03-10
    Description: Familial advanced sleep phase syndrome (FASPS) is an autosomal dominant circadian rhythm variant; affected individuals are "morning larks" with a 4-hour advance of the sleep, temperature, and melatonin rhythms. Here we report localization of the FASPS gene near the telomere of chromosome 2q. A strong candidate gene (hPer2), a human homolog of the period gene in Drosophila, maps to the same locus. Affected individuals have a serine to glycine mutation within the casein kinase Iepsilon (CKIepsilon) binding region of hPER2, which causes hypophosphorylation by CKIepsilon in vitro. Thus, a variant in human sleep behavior can be attributed to a missense mutation in a clock component, hPER2, which alters the circadian period.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Toh, K L -- Jones, C R -- He, Y -- Eide, E J -- Hinz, W A -- Virshup, D M -- Ptacek, L J -- Fu, Y H -- HL/HD 59596/HL/NHLBI NIH HHS/ -- M01-RR00064/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2001 Feb 9;291(5506):1040-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics, University of Utah, Salt Lake City, UT 84112, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11232563" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Binding Sites ; Biological Clocks/*genetics ; Casein Kinases ; Chromosome Mapping ; Chromosomes, Human, Pair 2/genetics ; Circadian Rhythm/*genetics ; Exons ; Female ; Genetic Linkage ; Glycine ; Humans ; Male ; Molecular Sequence Data ; Mutation, Missense ; Nuclear Proteins/chemistry/*genetics/*metabolism ; Pedigree ; Period Circadian Proteins ; Phosphorylation ; Polymorphism, Single-Stranded Conformational ; Protein Kinases/metabolism ; Proteins/chemistry/*genetics/*metabolism ; Serine ; Sleep Disorders, Circadian Rhythm/*genetics/physiopathology ; Transcription Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
    Publication Date: 1992-07-03
    Description: A proteinaceous elicitor of the plant defense reaction known as the hypersensitive response was isolated from Erwinia amylovora, the bacterium that causes fire blight of pear, apple, and other rosaceous plants. The elicitor, named harpin, is an acidic, heat-stable, cell-envelope-associated protein with an apparent molecular weight of 44 kilodaltons. Harpin caused tobacco leaf lamina to collapse and caused an increase in the pH of bathing solutions of suspension-cultured tobacco cells. The gene encoding harpin (hrpN) was located in the 40-kilobase hrp gene cluster of E. amylovora, sequenced, and mutated with Tn5tac1. The hrpN mutants were not pathogenic to pear, did not elicit the hypersensitive response, and did not produce harpin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wei, Z M -- Laby, R J -- Zumoff, C H -- Bauer, D W -- He, S Y -- Collmer, A -- Beer, S V -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):85-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Pathology, Cornell University, Ithaca, NY 14853.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1621099" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Bacterial Outer Membrane Proteins ; Bacterial Proteins/*genetics/isolation & purification/metabolism ; Cells, Cultured ; Erwinia/genetics/pathogenicity/*physiology ; Escherichia coli/genetics ; *Genes, Bacterial ; Membrane Proteins/*genetics/isolation & purification/metabolism ; Molecular Sequence Data ; *Multigene Family ; Plants, Toxic ; Restriction Mapping ; Tobacco/microbiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 2006-07-15
    Description: Plants have evolved a powerful immune system to defend against infection by most microbial organisms. However, successful pathogens, such as Pseudomonas syringae, have developed countermeasures and inject virulence proteins into the host plant cell to suppress immunity and cause devastating diseases. Despite intensive research efforts, the molecular targets of bacterial virulence proteins that are important for plant disease development have remained obscure. Here, we show that a conserved P. syringae virulence protein, HopM1, targets an immunity-associated protein, AtMIN7, in Arabidopsis thaliana. HopM1 mediates the destruction of AtMIN7 via the host proteasome. Our results illustrate a strategy by which a bacterial pathogen exploits the host proteasome to subvert host immunity and causes infection in plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nomura, Kinya -- Debroy, Sruti -- Lee, Yong Hoon -- Pumplin, Nathan -- Jones, Jonathan -- He, Sheng Yang -- New York, N.Y. -- Science. 2006 Jul 14;313(5784):220-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, MI 48824, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16840699" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factors/metabolism ; Arabidopsis/*immunology/metabolism/*microbiology ; Arabidopsis Proteins/*metabolism ; Bacterial Proteins/genetics/metabolism ; Brefeldin A/pharmacology ; Glucans/metabolism ; Guanine Nucleotide Exchange Factors/metabolism ; Immunity, Innate ; Mutation ; Plant Diseases/*microbiology ; Plant Leaves/metabolism/microbiology ; Plants, Genetically Modified ; Proteasome Endopeptidase Complex/metabolism ; Protein Transport ; Pseudomonas syringae/genetics/growth & development/*pathogenicity ; Tobacco/metabolism ; Two-Hybrid System Techniques ; Ubiquitins/metabolism ; Virulence Factors/genetics/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 2006-12-02
    Description: We describe a transgenesis platform for Drosophila melanogaster that integrates three recently developed technologies: a conditionally amplifiable bacterial artificial chromosome (BAC), recombineering, and bacteriophage PhiC31-mediated transgenesis. The BAC is maintained at low copy number, facilitating plasmid maintenance and recombineering, but is induced to high copy number for plasmid isolation. Recombineering allows gap repair and mutagenesis in bacteria. Gap repair efficiently retrieves DNA fragments up to 133 kilobases long from P1 or BAC clones. PhiC31-mediated transgenesis integrates these large DNA fragments at specific sites in the genome, allowing the rescue of lethal mutations in the corresponding genes. This transgenesis platform should greatly facilitate structure/function analyses of most Drosophila genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Venken, Koen J T -- He, Yuchun -- Hoskins, Roger A -- Bellen, Hugo J -- GM067858-05/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 15;314(5806):1747-51. Epub 2006 Nov 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Developmental Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17138868" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; *Chromosomes, Artificial, Bacterial ; Cloning, Molecular/*methods ; DNA Repair ; *DNA Transposable Elements ; Drosophila melanogaster/*genetics ; *Gene Transfer Techniques ; Genes, Insect ; Genetic Vectors ; Molecular Sequence Data ; Mutagenesis ; Plasmids ; Recombination, Genetic ; Siphoviridae/*genetics ; Transgenes ; Transposases/metabolism
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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