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A review of flexibility of residential electricity demand as climate solution in four EU countries 期刊论文
ENVIRONMENTAL RESEARCH LETTERS, 2020, 15 (7)
作者:  Mata, Erika;  Ottosson, Jonas;  Nilsson, Johanna
收藏  |  浏览/下载:18/0  |  提交时间:2020/08/18
demand side management  flexibility  grid edge  residential buildings  mitigation potentials  electricity demand  
The economic impacts of water supply restrictions due to climate and policy change: A transboundary river basin supply-side input-output analysis 期刊论文
ECOLOGICAL ECONOMICS, 2020, 172
作者:  Eamen, Leila;  Brouwer, Roy;  Razavi, Saman
收藏  |  浏览/下载:12/0  |  提交时间:2020/07/02
Supply-side input-output model  Transboundary river basin  Water supply restriction  Climate change  Economic impacts  Water policy  
The Deformational Journey of the Nazca Slab From Seismic Anisotropy 期刊论文
GEOPHYSICAL RESEARCH LETTERS, 2020, 47 (11)
作者:  Agrawal, Shubham;  Eakin, Caroline M.;  Portner, Daniel E.;  Rodriguez, Emily E.;  Beck, Susan L.
收藏  |  浏览/下载:8/0  |  提交时间:2020/05/13
Nazca slab  seismic anisotropy  source side splitting  slab anisotropy  slab deformation  
Accelerated discovery of CO2 electrocatalysts using active machine learning 期刊论文
NATURE, 2020, 581 (7807) : 178-+
作者:  Lan, Jun;  Ge, Jiwan;  Yu, Jinfang;  Shan, Sisi;  Zhou, Huan;  Fan, Shilong;  Zhang, Qi;  Shi, Xuanling;  Wang, Qisheng;  Zhang, Linqi;  Wang, Xinquan
收藏  |  浏览/下载:89/0  |  提交时间:2020/07/03

The rapid increase in global energy demand and the need to replace carbon dioxide (CO2)-emitting fossil fuels with renewable sources have driven interest in chemical storage of intermittent solar and wind energy(1,2). Particularly attractive is the electrochemical reduction of CO2 to chemical feedstocks, which uses both CO2 and renewable energy(3-8). Copper has been the predominant electrocatalyst for this reaction when aiming for more valuable multi-carbon products(9-16), and process improvements have been particularly notable when targeting ethylene. However, the energy efficiency and productivity (current density) achieved so far still fall below the values required to produce ethylene at cost-competitive prices. Here we describe Cu-Al electrocatalysts, identified using density functional theory calculations in combination with active machine learning, that efficiently reduce CO2 to ethylene with the highest Faradaic efficiency reported so far. This Faradaic efficiency of over 80 per cent (compared to about 66 per cent for pure Cu) is achieved at a current density of 400 milliamperes per square centimetre (at 1.5 volts versus a reversible hydrogen electrode) and a cathodic-side (half-cell) ethylene power conversion efficiency of 55 +/- 2 per cent at 150 milliamperes per square centimetre. We perform computational studies that suggest that the Cu-Al alloys provide multiple sites and surface orientations with near-optimal CO binding for both efficient and selective CO2 reduction(17). Furthermore, in situ X-ray absorption measurements reveal that Cu and Al enable a favourable Cu coordination environment that enhances C-C dimerization. These findings illustrate the value of computation and machine learning in guiding the experimental exploration of multi-metallic systems that go beyond the limitations of conventional single-metal electrocatalysts.


  
Molecular basis of beta-arrestin coupling to formoterol-bound beta(1)-adrenoceptor 期刊论文
NATURE, 2020
作者:  Pulliainen, Jouni;  Luojus, Kari;  Derksen, Chris;  Mudryk, Lawrence;  Lemmetyinen, Juha;  Salminen, Miia;  Ikonen, Jaakko;  Takala, Matias;  Cohen, Juval;  Smolander, Tuomo;  Norberg, Johannes
收藏  |  浏览/下载:29/0  |  提交时间:2020/07/03

The beta(1)-adrenoceptor (beta(1)AR) is a G-protein-coupled receptor (GPCR) that couples(1)to the heterotrimeric G protein G(s). G-protein-mediated signalling is terminated by phosphorylation of the C terminus of the receptor by GPCR kinases (GRKs) and by coupling of beta-arrestin 1 (beta arr1, also known as arrestin 2), which displaces G(s)and induces signalling through the MAP kinase pathway(2). The ability of synthetic agonists to induce signalling preferentially through either G proteins or arrestins-known as biased agonism(3)-is important in drug development, because the therapeutic effect may arise from only one signalling cascade, whereas the other pathway may mediate undesirable side effects(4). To understand the molecular basis for arrestin coupling, here we determined the cryo-electron microscopy structure of the beta(1)AR-beta arr1 complex in lipid nanodiscs bound to the biased agonist formoterol(5), and the crystal structure of formoterol-bound beta(1)AR coupled to the G-protein-mimetic nanobody(6)Nb80. beta arr1 couples to beta(1)AR in a manner distinct to that(7)of G(s)coupling to beta(2)AR-the finger loop of beta arr1 occupies a narrower cleft on the intracellular surface, and is closer to transmembrane helix H7 of the receptor when compared with the C-terminal alpha 5 helix of G(s). The conformation of the finger loop in beta arr1 is different from that adopted by the finger loop of visual arrestin when it couples to rhodopsin(8). beta(1)AR coupled to beta arr1 shows considerable differences in structure compared with beta(1)AR coupled to Nb80, including an inward movement of extracellular loop 3 and the cytoplasmic ends of H5 and H6. We observe weakened interactions between formoterol and two serine residues in H5 at the orthosteric binding site of beta(1)AR, and find that formoterol has a lower affinity for the beta(1)AR-beta arr1 complex than for the beta(1)AR-G(s)complex. The structural differences between these complexes of beta(1)AR provide a foundation for the design of small molecules that could bias signalling in the beta-adrenoceptors.


A cryo-electron microscopy structure of the beta 1-adrenoceptor coupled to beta-arrestin 1 and activated by the biased agonist formoterol, as well as the crystal structure of a related formoterol-bound adrenoreceptor, provide insights into biased signalling in these systems.


  
Entanglement-based secure quantum cryptography over 1,120 kilometres 期刊论文
NATURE, 2020
作者:  Paldi, Flora;  Alver, Bonnie;  Robertson, Daniel;  Schalbetter, Stephanie A.;  Kerr, Alastair;  Kelly, David A.;  Baxter, Jonathan;  Neale, Matthew J.;  Marston, Adele L.
收藏  |  浏览/下载:48/0  |  提交时间:2020/07/03

An efficient entanglement-based quantum key distribution is sent from the Micius satellite to two ground observatories 1,120 kilometres apart to establish secure quantum cryptography for the exchange ofquantum keys.


Quantum key distribution (QKD)(1-3)is a theoretically secure way of sharing secret keys between remote users. It has been demonstrated in a laboratory over a coiled optical fibre up to 404 kilometres long(4-7). In the field, point-to-point QKD has been achieved from a satellite to a ground station up to 1,200 kilometres away(8-10). However, real-world QKD-based cryptography targets physically separated users on the Earth, for which the maximum distance has been about 100 kilometres(11,12). The use of trusted relays can extend these distances from across a typical metropolitan area(13-16)to intercity(17)and even intercontinental distances(18). However, relays pose security risks, which can be avoided by using entanglement-based QKD, which has inherent source-independent security(19,20). Long-distance entanglement distribution can be realized using quantum repeaters(21), but the related technology is still immature for practical implementations(22). The obvious alternative for extending the range of quantum communication without compromising its security is satellite-based QKD, but so far satellite-based entanglement distribution has not been efficient(23)enough to support QKD. Here we demonstrate entanglement-based QKD between two ground stations separated by 1,120 kilometres at a finite secret-key rate of 0.12 bits per second, without the need for trusted relays. Entangled photon pairs were distributed via two bidirectional downlinks from the Micius satellite to two ground observatories in Delingha and Nanshan in China. The development of a high-efficiency telescope and follow-up optics crucially improved the link efficiency. The generated keys are secure for realistic devices, because our ground receivers were carefully designed to guarantee fair sampling and immunity to all known side channels(24,25). Our method not only increases the secure distance on the ground tenfold but also increases the practical security of QKD to an unprecedented level.


  
Structural basis for catalysis and substrate specificity of human ACAT1 期刊论文
NATURE, 2020, 581 (7808) : 333-+
作者:  Jiao, Huipeng;  Wachsmuth, Laurens;  Kumari, Snehlata;  Schwarzer, Robin;  Lin, Juan;  Eren, Remzi Onur;  Fisher, Amanda;  Lane, Rebecca;  Young, George R.;  Kassiotis, George;  Kaiser, William J.;  Pasparakis, Manolis
收藏  |  浏览/下载:10/0  |  提交时间:2020/07/03

The structure of human ACAT1, which catalyses the transfer of an acyl group from acyl-coenzyme A to cholesterol to form cholesteryl ester, is resolved by cryo-electron microscopy.


As members of the membrane-bound O-acyltransferase (MBOAT) enzyme family, acyl-coenzyme A:cholesterol acyltransferases (ACATs) catalyse the transfer of an acyl group from acyl-coenzyme A to cholesterol to generate cholesteryl ester, the primary form in which cholesterol is stored in cells and transported in plasma(1). ACATs have gained attention as potential drug targets for the treatment of diseases such as atherosclerosis, Alzheimer'  s disease and cancer(2-7). Here we present the cryo-electron microscopy structure of human ACAT1 as a dimer of dimers. Each protomer consists of nine transmembrane segments, which enclose a cytosolic tunnel and a transmembrane tunnel that converge at the predicted catalytic site. Evidence from structure-guided mutational analyses suggests that acyl-coenzyme A enters the active site through the cytosolic tunnel, whereas cholesterol may enter from the side through the transmembrane tunnel. This structural and biochemical characterization helps to rationalize the preference of ACAT1 for unsaturated acyl chains, and provides insight into the catalytic mechanism of enzymes within the MBOAT family(8).


  
Convergent genes shape budding yeast pericentromeres 期刊论文
NATURE, 2020
作者:  Yin, Xuefan;  Jin, Jicheng;  Soljacic, Marin;  Peng, Chao;  Zhen, Bo
收藏  |  浏览/下载:25/0  |  提交时间:2020/07/03

The three-dimensional structure of pericentromeres in budding yeast is defined by convergent genes, which mark pericentromere borders and trap cohesin complexes loaded at centromeres, generating an architecture that allows correct chromosome segregation.


The three-dimensional architecture of the genome governs its maintenance, expression and transmission. The cohesin protein complex organizes the genome by topologically linking distant loci, and is highly enriched in specialized chromosomal domains surrounding centromeres, called pericentromeres(1-6). Here we report the three-dimensional structure of pericentromeres in budding yeast (Saccharomyces cerevisiae) and establish the relationship between genome organization and function. We find that convergent genes mark pericentromere borders and, together with core centromeres, define their structure and function by positioning cohesin. Centromeres load cohesin, and convergent genes at pericentromere borders trap it. Each side of the pericentromere is organized into a looped conformation, with border convergent genes at the base. Microtubule attachment extends a single pericentromere loop, size-limited by convergent genes at its borders. Reorienting genes at borders into a tandem configuration repositions cohesin, enlarges the pericentromere and impairs chromosome biorientation during mitosis. Thus, the linear arrangement of transcriptional units together with targeted cohesin loading shapes pericentromeres into a structure that is competent for chromosome segregation. Our results reveal the architecture of the chromosomal region within which kinetochores are embedded, as well as the restructuring caused by microtubule attachment. Furthermore, we establish a direct, causal relationship between the three-dimensional genome organization of a specific chromosomal domain and cellular function.


  
The architecture of the Gram-positive bacterial cell wall 期刊论文
NATURE, 2020, 582 (7811) : 294-+
作者:  Farquharson, Jamie I.;  Amelung, Falk
收藏  |  浏览/下载:25/0  |  提交时间:2020/07/03

The primary structural component of the bacterial cell wall is peptidoglycan, which is essential for viability and the synthesis of which is the target for crucial antibiotics(1,2). Peptidoglycan is a single macromolecule made of glycan chains crosslinked by peptide side branches that surrounds the cell, acting as a constraint to internal turgor(1,3). In Gram-positive bacteria, peptidoglycan is tens of nanometres thick, generally portrayed as a homogeneous structure that provides mechanical strength(4-6). Here we applied atomic force microscopy(7-12) to interrogate the morphologically distinct Staphylococcus aureus and Bacillus subtilis species, using live cells and purified peptidoglycan. The mature surface of live cells is characterized by a landscape of large (up to 60 nm in diameter), deep (up to 23 nm) pores constituting a disordered gel of peptidoglycan. The inner peptidoglycan surface, consisting of more nascent material, is much denser, with glycan strand spacing typically less than 7 nm. The inner surface architecture is location dependent  the cylinder of B. subtilis has dense circumferential orientation, while in S. aureus and division septa for both species, peptidoglycan is dense but randomly oriented. Revealing the molecular architecture of the cell envelope frames our understanding of its mechanical properties and role as the environmental interface(13,14), providing information complementary to traditional structural biology approaches.


Using high-resolution atomic force microscopy of live cells, the authors present an updated view of the cell walls of both Staphylococcus aureus and Bacillus subtilis.


  
Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme 期刊论文
NATURE, 2020, 581 (7808) : 323-+
作者:  Nikoo, Mohammad Samizadeh;  Jafari, Armin;  Perera, Nirmana;  Zhu, Minghua;  Santoruvo, Giovanni;  Matioli, Elison
收藏  |  浏览/下载:19/0  |  提交时间:2020/07/03

Triacylglycerols store metabolic energy in organisms and have industrial uses as foods and fuels. Excessive accumulation of triacylglycerols in humans causes obesity and is associated with metabolic diseases(1). Triacylglycerol synthesis is catalysed by acyl-CoA diacylglycerol acyltransferase (DGAT) enzymes(2-4), the structures and catalytic mechanisms of which remain unknown. Here we determined the structure of dimeric human DGAT1, a member of the membrane-bound O-acyltransferase (MBOAT) family, by cryo-electron microscopy at approximately 3.0 angstrom resolution. DGAT1 forms a homodimer through N-terminal segments and a hydrophobic interface, with putative active sites within the membrane region. A structure obtained with oleoyl-CoA substrate resolved at approximately 3.2 angstrom shows that the CoA moiety binds DGAT1 on the cytosolic side and the acyl group lies deep within a hydrophobic channel, positioning the acyl-CoA thioester bond near an invariant catalytic histidine residue. The reaction centre is located inside a large cavity, which opens laterally to the membrane bilayer, providing lipid access to the active site. A lipid-like density-possibly representing an acyl-acceptor molecule-is located within the reaction centre, orthogonal to acyl-CoA. Insights provided by the DGAT1 structures, together with mutagenesis and functional studies, provide the basis for a model of the catalysis of triacylglycerol synthesis by DGAT.


Cryo-electron microscopy structures and functional and mutagenesis studies provide insights into the catalysis of triacylglycerol synthesis by human acyl-CoA diacylglycerol acyltransferase at its intramembrane active site.