Tag: 苏州桑拿

Tottenham title pursuit goes on

first_imgLONDON (AP): Tottenham kept up their pursuit of Premier League leaders Leicester by rallying to a 2-1 victory over Swansea, thanks to two goals in eight minutes yesterday. Left back Danny Rose was the surprise match-winner for Spurs, scoring in the 77th minute after Swansea failed to clear a corner properly. Tottenham had 34 attempts on goal, prompting their manager Mauricio Pochettino to tell Spurs TV: “What more you need to do for (to) score? … This is the way that we want to play and you know sometimes football is not mathematical.” Nacer Chadli cancelled out Swansea’s opener by Alberto Paloschi in the 19th minute as the visitors paid for their defensive approach in the second half at White Hart Lane. Pochettino praised Spurs fans for lifting the team after Swansea went ahead. “This was very important for us,” Pochettino said. “‘Thank you’, our supporters. They were brilliant. And ‘thank you’, the players, because the performance and the effort was unbelievable after that Europa League game (Thursday) against Fiorentina.”last_img read more

DD Gardening: The Importance of planting a hedging

first_imgHave you considered planting a hedge in your garden? If you have then Donegal Daily’s horticulture specialist Conor Gallinagh gives you the low down on the steps you need to take below. A hedge, in my opinion, benefits the garden in these ways.Creates a backdrop or framework to work from for the rest of your garden.Provides shelter to the garden and houseCreates an ecosystem for wildlifeThe bareroot season is an ideal time to plant your hedge. Of old it was defined as any month with an ‘R’. As our climate changes the season has drawing shorter normally now from November to Mid-April. Advertisement So we still have some time left to get that hedge planted or even begin planning for the next season.Bareroot simple means that the plant is dormant and without a growing medium i.e. roots exposed.Donegal proves to be a difficult county to grow plants. Going from windswept coastal garden’s to bog covered lands to fertile valleys all within a couple of kilometres of each other.The soils greatly dictate the variety best suited as well as the climate and client’s personal taste also play a role. Advertisement Here are some of my recommendation for the different locations that can be found.Fertile Soils in Lowlands Beech – Fagus sylvatica This forms into a really beautiful natural hedge. In non-windswept areas, the dormant leaves will cling on over the winter to give a beautiful bronze effect. The glossy light green leaves unfold from pointed buds in spring and as the season transforms they darken to a richer green hue.Fertile Soils Highland. (Evergreen hedge) Common Laurel – Prunus laurocerasusA reliable classic evergreen hedge. Can withstand a range of soils and environments. The long dark glossy leaves remain throughout the year. Forms into a tight compact hedge.Poor Soils Hornbeam – Carpinus betulus This species is often confused with beech as it has a similar leaf and growth habitat. Look a little closer and you will see deep groves or ridges running through the leaves, unlike the smooth beech leaf. It’s also missing the distinctive pointed orange-red buds of Beech. Unlike the Beech as well the Hornbeam will grow quite successfully on poor or less fertile soils. Coastal HedgeGriselinia littoralisThe foliage has a rubber texture and completely smooth which it makes it very suitable for the salt-laden breeze along the coast. An evergreen with light green smooth leaves. Does well in sandy soils.Biodiversity Hedge Hawthorn – Crataegus monogynaUsing Hawthorn as your base plant, interplant with species of Holly, Wild Cherry, Guelder Rose and Dogrose. This will provide a hedge where an ecosystem should thrive in and also provide interest all year round.A Bit Different Perhaps you’re looking for something that little bit different. The Photina varieties, in particular, ‘Red Robin’ or ‘Magical Volcano’ could be an option.In my opinion, the new variety ‘Magical Volcano’ has the potential to make a wonderful hedge. The bright red juvenile foliage with its crinkled edging is a real eye-catcher.It also has a much denser growing habitat than its counterparts. One to watch for sure.Boxwood Alternative With Buxus sempervirens suffering from various disease and becoming a little bit old fashioned, the search is on to find an alternative.The Ilex crenata, in my opinion, seems to be a suitable replacement. A similar leaf structure, growth habit and shape. Seems to match up the criteria well.Just remember that the end of the bareroot is coming in fast. Once it ends my recommendation is to hold off until it starts in November again.Use the time in between to plan the area, choose the species you wish to grow and order them in advance as well.Any questions on this column or looking for further advice either send me an email at [email protected] or message me over on my Facebook page Conor Gallinagh – Horticulture Consultant.Happy Gardening!DD Gardening: The Importance of planting a hedging was last modified: March 24th, 2019 by Conor GallinaghShare this:Click to share on Facebook (Opens in new window)Click to share on Twitter (Opens in new window)Click to share on LinkedIn (Opens in new window)Click to share on Reddit (Opens in new window)Click to share on Pocket (Opens in new window)Click to share on Telegram (Opens in new window)Click to share on WhatsApp (Opens in new window)Click to share on Skype (Opens in new window)Click to print (Opens in new window)Tags:Conor Gallinaghdd gardeninghorticulturelast_img read more

Cell Chaperones Keep Proteins Properly Folded

first_imgImagine linking together a chain of 300 plastic shapes, some with magnets at various places.  Then let it go and see if you could get it to fold spontaneously into a teapot.  This is the challenge that cells face every minute: folding long chains of amino acids (polypeptides) into molecular machines and structures for the cell’s numerous tasks required for life.  DNA in the nucleus codes for these polypeptides.  They are assembled in ribosomes in single-file order.  How do they end up in complex folded shapes?  Some polypeptides will spontaneously collapse into their native folds, like the magnetic chain in our analogy.  Others, however, need help.  Fortunately, the cell provides an army of assistants, called chaperones, to monitor, coax, and repair unfolded proteins, to achieve “proteostasis” – a stable, working set of proteins.  That army is so well-organized and complex, scientists continue to try to figure out how it performs so well in the field. Polypeptide chains don’t have magnets, but they have amino acids that produce other forces: side chains that are hydrophilic (water-loving) or hydrophobic (water-repelling), side chains that are acidic or basic, and side chains that are attracted chemically to certain other amino acids.  Let some of these chains go in a test tube and they will spontaneously fold properly because of the precise way they were coded by DNA.  Others require the help of chaperones to fold.  In a review article last week in Nature,1 Hartl, Bracher and Hayer-Hartl from the Max Planck Institute surveyed what is currently known about protein chaperones.  The importance of proteostasis is evident in their first paragraph: Most proteins must fold into defined three-dimensional structures to gain functional activity. But in the cellular environment, newly synthesized proteins are at great risk of aberrant folding and aggregation, potentially forming toxic species. To avoid these dangers, cells invest in a complex network of molecular chaperones, which use ingenious mechanisms to prevent aggregation and promote efficient folding. Because protein molecules are highly dynamic, constant chaperone surveillance is required to ensure protein homeostasis (proteostasis). Recent advances suggest that an age-related decline in proteostasis capacity allows the manifestation of various protein-aggregation diseases, including Alzheimer’s disease and Parkinson’s disease. Interventions in these and numerous other pathological states may spring from a detailed understanding of the pathways underlying proteome maintenance. Our mammalian cells typically assemble 10,000 different types of proteins.  How they fold properly is “one of the most fundamental and medically relevant problems in biology,” the authors said.  The folded states, furthermore, must be loose enough in many cases to allow for movements (conformational changes) that are essential to their functions.  Thus, protein quality control and the maintenance of proteome homeostasis (known as proteostasis) are crucial for cellular and organismal health.  Proteostasis is achieved by an integrated network of several hundred proteins, including, most prominently, molecular chaperones and their regulators, which assist in de novo folding or refolding, and the ubiquitin–proteasome system (UPS) and autophagy system, which mediate the timely removal of irreversibly misfolded and aggregated proteins. Each polypeptide has to navigate a complex “folding-energy landscape” to find its native fold – something like a golf ball in a miniature golf game having to go up, down, and around a series of obstacles to land in the hole.  Simple polypeptides with simple landscapes can often find their fold in millionths of a second in a test tube environment.  Larger, complex ones can take minutes or even hours.  In the cell, it’s even more difficult, owing to the crowded environment of many kinds of molecules bouncing around.  Without the chaperone system, many of the contacts would lead to aggregates of useless or even toxic peptides, like golf balls accumulating in the wrong dip on the landscape, unable to get out.  Chaperones can nudge them out of their traps and back toward the hole. What do the chaperones look like?  In the diagrams the authors provided, some look like clamps; in fact, the authors called HSP90 a “molecular clamp” that is able to free up stuck proteins and let them proceed to their native folds.  HSP90 requires ATP and a suite of cofactors and regulators to work.  That’s just one of hundreds of chaperone types. When peptide chains emerge from the ribosome, there’s a risk they will start folding too early at the leading edge.  Folding needs to wait till the tail end gets out of the tunnel.  (Translation, the authors say, proceeds “relatively slow” at 4 to 20 amino acids per second in eukaryotes and bacteria, respectively.)  Premature folding is inhibited by ribosome complexes that arrange multiple ribosomes in ways that maximize the distance between nascent chains, and by ribosome-bound chaperones that monitor and protect the nascent chains till they fully exit the tunnel. Another challenge cells face is organizing proteins that have multiple domains.  These domains may exit the ribosome separately, but need to be brought together for final assembly.  In such cases, whole chaperone complexes may be involved in post-translational assembly.  These systems are so finely tuned, they can take advantage of pauses at rare codons in the ribosome to achieve co-translational folding.  “Overall,” they remarked, “the eukaryotic translation and chaperone machinery has been highly optimized through evolution, ensuring efficient folding for the bulk of newly synthesized proteins.”  Further chaperone duty awaits at the endoplasmic reticulum: “The chaperone pathways operating in the endoplasmic reticulum (ER) follow analogous organizational principles, but specialized machinery is used in disulphide-bond formation and the glycosylation of many secretory proteins.” Once proteins are folded properly, the chaperone army’s work is not done.  Protein surveillance machines monitor the proteome and deal with proteins that start to unfold or otherwise go awry.  “Although it is generally accepted that the chaperone machinery is required for initial protein folding,” they said, “we are only beginning to appreciate the extent to which many proteins depend on macromolecular assistance throughout their cellular lifetime to maintain or regain their functionally active conformations.”  This is especially true in eukaryotes, which have a “much greater number and diversity of multidomain proteins.”  Think of all that can go wrong: In the dynamic cellular environment, these proteins constantly face numerous challenges to their folded states; these result from post-translational modifications (phosphorylation and acetylation), changes in cell physiology and alterations in the composition and concentration of small-molecule ligands that may influence protein stability. Moreover, 20-30% of all proteins in mammalian cells are intrinsically unstructured; that is, they may adopt defined three-dimensional conformations only after binding to other macromolecules or membrane surfaces. Such proteins probably require assistance to avoid aberrant interactions and aggregation, particularly when their concentration is increased and they are not in complexes with partner molecules. To maintain proteostasis, the cell employs some 200 chaperones and co-chaperones and 600 other machines concerned with trash collection and recycling.  The barrel-shaped chaperone Gro-EL/Gro-ES in bacteria, which provides a protein “dressing room” with lid, has an even more complex counterpart in eukaryotes called TRiC with an “iris-like, built in lid” for privacy, allowing even more time for the encaged protein to try to fold properly.  “TRiC interacts with approximately 10% of newly synthesized cytosolic proteins, including actin and tubulins,” they said.  “Interestingly, TRiC also functions in preventing the accumulation of toxic aggregates by the Huntington’s disease protein.”  Another family are the heat-shock proteins (HSP) that are up-regulated in times of cellular stress.  “They are involved in a multitude of proteome-maintenance functions, including de novo folding, refolding of stress-denatured proteins, oligomeric assembly, protein trafficking and assistance in proteolytic degradation.”  HSP90, the one mentioned earlier, is a “proteostasis hub” with multiple jobs: “cell-cycle progression, telomere maintenance, apoptosis, mitotic signal transduction, vesicle-mediated transport, innate immunity and targeted protein degradation.” The authors concluded by discussing some of the diseases that occur when chaperones fail, and how ageing itself might be a result of decreasing chaperone function that leads to aggregation of useless protein fragments.  There is still a great deal to learn about chaperones.  “Key questions include determining how certain aberrantly folding proteins aggregate into toxic species whereas others are degraded, how the composition of the proteosome changes during ageing, what the signature of a youthful proteome is, and how we can find ways to maintain it for longer as we age.” How did this elaborate quality-control system arise?  The authors mentioned evolution six times, but not once did they explain a plausible pathway from early life without chaperones to life with them (which is true in all three kingdoms of life, archaea, bacteria and eukaryotes).  They merely assumed evolution invented these machines because cells needed them: “It seems likely, therefore, that the fundamental requirement for molecular chaperones arose very early during the evolution of densely crowded cells, owing to the need to minimize protein aggregation during folding and maintain proteins in soluble, yet conformationally dynamic states.”  They suggested that chaperones might aid evolution: “Moreover, as mutations often disrupt the ability of a protein to adopt a stable fold, it follows that the chaperone system provides a crucial buffer, allowing the evolution of new protein functions and phenotypic traits.”  No examples of this were provided; just vague suggestions: “the evolution and maintenance of these functional networks is thought to depend on the ability of HSP90 to buffer the effects of structurally destabilizing mutations in the underlying protein complexes, thereby allowing the acquisition of new traits.”  Thus, it might act as a kind of “evolutionary capacitor in protecting mutated protein variants from degradation.”  This seems an odd suggestion, since the role of chaperones is to maintain proteostasis.  Nevertheless, they piled on more suggestions: “Sequential domain folding during translation, which is highly efficient on eukaryotic ribosomes, probably promoted the explosive evolution of complex multidomain proteins in eukaryotes.” In short, though, they could not deny that “the eukaryotic translation and chaperone machinery has been highly optimized through evolution, ensuring efficient folding for the bulk of newly synthesized proteins.”  Everyone can agree on the optimization without necessarily agreeing on the mechanism of evolution. 1.  F. Ulrich Hartl, Andreas Bracher, and Manajit Hayer-Hartl, “Molecular chaperones in protein folding and proteostasis,” Nature 475  (21 July 2011), pp. 324–332, doi:10.1038/nature10317. This is a fascinating review paper worth reading for the marvelous realities revealed that go on every minute of every day, silently, inside our bodies.  Just hold your nose at the occasional evolutionary stories and you will be blessed.(Visited 54 times, 1 visits today)FacebookTwitterPinterestSave分享0last_img read more

Commercial Net-Zero Buildings On the Rise

first_imgAlthough the numbers are still very small, proven net-zero energy performance in commercial buildings is rising at a statistically rapid pace, a report from the New Buildings Institute says.Over a 15-month period, the number of verified “ZE” projects rose from 53 to 67, an increase of 26%. A much broader category of “emerging” commercial buildings that includes projects under construction, in design and still being evaluated climbed from 279 to 415, an increase of more than 48%, the report said.There are 6 million commercial buildings in the U.S. and Canada, so the number of projects capable of balancing energy consumption with production from renewable energy sources over the course of a year is barely a drop in the bucket. But it’s the rate of increase and a “convergence” of factors that favor zero-energy design the institute finds significant. In the first of these reports in 2012, the institute said, there were a total of 60 commercial and multifamily projects that could be listed as verified or in the works. With that number now 482, the total has increased by more than 700%.“ZE buildings counts are still small in relation to the total market — in the single-digit percentage of total buildings and floor space,” the report says. “But a multitude of factors are accelerating ZE buildings and communities such as emerging technologies, sensors and LEDs, dramatic price drops of solar generation, energy storage, energy tracking and transparency, integrated and passive design, climate concerns, and interest in ZE codes and resilient buildings. How performance is definedThe New Building Institute uses a metric it calls the Zero Energy Performance Index, or zEPI, which favors actual energy consumption over an energy model of performance. The zEPI is calculated with the building’s EUI and is adjusted by building type and climate once a building is occupied based on measured energy use.The report explains zEPI this way:“ZEPI was created to address confusion caused by comparing the energy efficiency of buildings by referencing their ‘percent savings beyond code.’ Which code? What year? Given there have been at least six major commercial energy codes on the books at any given time in the United States since 2000, identifying the correct baseline can take some time.”This new report is for commercial buildings only. Residential net-zero projects are tallied separately by the Net-Zero Energy Coalition (see the Related Articles sidebar above for an article on its latest report), although some critics doubt it is possible to count zero-energy homes accurately because of the wide distribution of renewable energy systems. RELATED ARTICLES Projects of all types make the listWhen organized by building type, education represents the largest group with 37% of the total. Office buildings and multifamily make up the next two in the rankings with 19% and 16% respectively. But developers of all stripes are showing interest in the zero-energy standard, the report says, with light manufacturing, a car dealership and a ski area making the list. Healthcare, lodging, and retail stores are categories with relatively little representation, possibly because of higher energy intensity and more complicated use patterns.The report also makes these observations:In addition to buildings whose developers expressly list zero-net energy as a goal, there are many others listed as “ultra-low energy buildings,” which achieve similar levels of energy performance without the addition of renewables and without having zero-energy goals. These projects are not included in the ZE tally because there are too many to list.There are zero-energy commercial projects in 44 U.S. states and four of Canada’s 10 provinces. California, however, has seen the most growth (131%) and with 214 projects it has 44% of the total. Taken together, California and Oregon account for just under half of the total. Other regions making a particularly strong showing are the Northeast (73 projects), the Southeast (50 projects) and the Southwest (41 projects). States with no ZE projects are North Dakota, South Dakota, Oklahoma, Louisiana, Mississippi, and Alaska.Zero-energy buildings can be found in all climate zones. But the largest grouping (226 projects) is located in Climate Zone 3, which extends across the southern tier of the U.S.Verified projects on the list use an average of 60% less energy that comparable commercial buildings in the U.S. The median gross site Energy Use Intensity (EUI) is just under 18kBtu/square foot/year before renewables are factored in. Those projects on the emerging list have an EUI of 24kBtu/square foot/year.Eighty-one percent of the verified buildings are 25,000 square feet or less in size, with the biggest concentration (31%) of 5,000 square feet or less. Less than 1% are bigger than 100,000 square feet. There’s better representation on the emerging side of the tally for larger buildings: 18% are larger than 100,000 square feet, and 23% are between 50,000 and 100,000 square feet.center_img To Net Zero and BeyondZero-Energy Construction is ‘Set to Explode’ The Department of Energy Chooses a Definition for Net ZeroMajor U.S. Builder Tests Net-Zero MarketNet-Zero Cities Aren’t Possible, You Say?California Leads the Nation in Net-Zero Projects “This convergence, combined with other rapid advancements, foretells of a built environment that will look very different when we share our story 20 years from now.”last_img read more

10 months agoREVEALED: Sevilla ace Banega changed agents to get Arsenal move

first_imgREVEALED: Sevilla ace Banega changed agents to get Arsenal moveby Paul Vegas10 months agoSend to a friendShare the loveSevilla ace Ever Banega has changed agents to secure a move to England, it has been revealed.Mundo Deportivo says Banega has recently brought in new representatives as he seeks a move to the Premier League.And his agent is spending time in London over the festive period to finalise a deal with Arsenal.Unai Emery and Banega enjoyed a good player coach relationship during spells at Valencia and Sevilla – where they won two Europa League titles in 2015 and 2016.Banega is now in his second spell with Sevilla, having played for the likes of Atletico Madrid and Inter Milan. The Arsenal boss sees the Argentine as the perfect candidate to fill the boots of Aaron Ramsey who could leave as soon as January. TagsTransfersAbout the authorPaul VegasShare the loveHave your saylast_img read more

10 months ago​Boussouma potential excites Brighton boss Hughton

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first_img​Boussouma potential excites Brighton boss Hughtonby Ansser Sadiq10 months agoSend to a friendShare the loveBrighton manager Chris Hughton is excited at the potential of Yves Bissouma.The Mali midfielder is already impressing for the Premier League side, scoring a long range goal in the FA Cup against Bournemouth.And Hughton believes that when his English improves, he will be fully integrated into the squad.Hughton told The Argus: “He is still learning. He is a wonderful talent, probably one of the most talented players that we’ve had here.”But it’s just about nurturing that one. He is still young, he is still learning the language and he will get better.”I hope so. The game, particularly in the position he plays, is about a lot of aspects and you have got to do enough of those aspects well.”At the moment he is still developing. I think once he gets a good grasp of the language he’ll improve.” About the authorAnsser SadiqShare the loveHave your saylast_img read more

10 months agoUNCOVERED: Real Madrid signing Brahim Diaz was Messi and Barcelona mad!

first_imgTagsTransfersAbout the authorCarlos VolcanoShare the loveHave your say UNCOVERED: Real Madrid signing Brahim Diaz was Messi and Barcelona mad!by Carlos Volcano10 months agoSend to a friendShare the loveReal Madrid signing Brahim Diaz grew up a Barcelona fan and idolising Leo Messi!Diaz left Manchester City to sign for Real this week.And a video has emerged which shows that Diaz hasn’t been a Los Blancos supporter all his life. Brahim, in an interview he gave at the age of 12, admitted that his favourite team was FC Barcelona and that his footballing idol was Messi.DOCUMENTO #JUGONES Cuándo tenía 12 años, Brahim era del Barça y su ÍDOLO era Messi! SE HARÁ VIRAL! Lo estamos viendo en @laSextaTV. pic.twitter.com/IAyTHQcYDs— El Chiringuito TV (@elchiringuitotv) January 8, 2019 last_img read more

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