A motorcyclist, who was reportedly speeding, was killed late Sunday evening after he fatally struck down an allegedly drunken pedestrian on the southern carriageway of the East Coast Demerara Highway. The accident occurred around 21:15h at Liliendaal, Greater Georgetown.The motorcycle involved in the accidentThe dead motorcyclist has been identified as 25-year-old Frank De Florimde Jr of Lot 61 Fourth Street, Sparendaam, East Coast Demerara. Meanwhile, the pedestrian, who was attempting to cross the road at the time of the accident, was unidentified up to press time Sunday night. However, Guyana Times understands that the man was known as “Buckman” and resided somewhere on Barr Street, Kitty.According to reports reaching this newspaper, De Florimde was riding motorcycle CH 7805 when he collided with the man. Guyana Times understands that after being struck, the pedestrian was dragged a short distance away.The motorcyclist, on the other hand, kept on sliding on the motorcycle before it came to a halt and he ended up on the middle of the roadway. When this newspaper arrived on the scene shortly after the accident, De Florimde was lying on the road in a pool of blood. An eyewitness related to this publication that he was driving his motor car when he saw the motorcycle speeding past him.“If I didn’t pull in the corner, I would have hit him,” the driver explained.Another eyewitness told Guyana Times that De Florimde jumped a traffic light at UG Road shortly before the accident.As news spread of the accident, distraught family and friends of the motorcyclist gathered at the scene.“Junior! Get up, let we go home!” one of the dead man’s sisters cried, hitting his chest.“I does be scared every time you go on the road…I don’t want tell you…Please get up…noo…don’t carry way my brother, please!” De Florimde’s sister screamed as undertakers tried to take him away.Meanwhile, De Florimde’s father told this publication, “I called my son and asked him where he was and he told me that he bathing. He didn’t tell me, he was going out on the seawall. I does tell this boy not to ride speed, but he don’t hear…He does do this for fun. You know how these young people stay.”
Corporate Guyana has thrown its support behind the National U20 Team as preparations continue for its successful participation in the CONCACAF U20 Men’s Championships, scheduled to be held from November 1st to 22nd in Florida, USA.The donations, respectively in the form of health supplements, snacks, water, a monetary and in-kind contribution, were received, and will assist team members in their daily preparations. The NEW GPC INC donated Codol Compound, which provides extra-strength and vitality while building resistance; and Mustarcream, which helps sore joints and muscles. Team Manager Daniel Thomas, expressing gratitude for the donations, has said the items received have contributed, and will greatly contribute, to the success of the programme.He also was very appreciative of donations received from other supporters, and expressed his appreciation accordingly. “We’re happy that Maggie’s Catering has come on board and provided snacks for a number of days, as well as offered a discount for snacks provided for the remainder of the month thus far. The Guyana Producers Limited, through Mr Aaron Fraser, has also given a financial donation. We have also had water being provided for the team through Mr. Clifton Douglas of Ultra Waters, which has resulted in us not paying for water for the past month through that kind sponsorship,” he disclosed.“St Joseph Mercy Hospital was also instrumental in facilitating…the team’s medicals, which (were) required by CONCACAF as a prerequisite for participation in the tournament,” he further disclosed.Daniels said the team, which is scheduled to depart on October 28, is also open to additional sponsorship.The National U20 Team’s match schedule in the first round will see it taking on Guatemala on November 2nd, the Cayman Islands on November 6th, Curacao on November 8th, and El Salvador on November 10th.
0Shares0000Sony Sugar’s Yema Mwana attempts an overhead kick under pressure from Sofapaka’s Bernard Mang’oli and Humphrey Okoti during a Kenyan Premier League match at the Ruaraka Complex on April 15, 2018. PHOTO/Timothy OlobuluNAIROBI, Kenya, Apr 15- A tale of two penalties saw 10-man Sony Sugar fight from a goal down to draw 1-1 with 2009 champions Sofapaka at the Ruaraka Complex on Sunday evening, handing John Baraza a stuttering start as Batoto ba Mungu head coach.Sofapaka scored in the first half via a Mathias Kigonya penalty and the sugar-belt side responded in the second half via David Simiyu, also from the penalty spot. Sony were reduced to 10 men early in the second half after Samuel Olare was sent off for elbowing an opponent. Batoto ba Mungu broke the deadlock on the half hour mark when Sony Sugar shot stopper Kevin Omondi bungled down Kepha Aswani from the back as the two of them went high to meet a cross from Brian Dayo.Just like he has done on three previous occasions already this season, goalkeeper Kigonya stepped forward to score the resultant spot kick.Sofapaka had duly gone ahead after dictating much of the tempo in the game, earning possession and passing the ball around the park well. Kigonya had seen less action on his end as Sony ended the opening half without a single shot on target.Baraza’s charges had their first effort at goal in the eighth minute when Dayo took a shot from distance after his side had built up play patiently, but the ball went over.New Sofapaka head coach John Baraza was well suited for the occasion on his first match in charge against Sony Sugar on April 15, 2018. PHOTO/Raymond MakhayaAswani had a great chance after 20 minutes when Willis Ouma’s cross from the right landed on his head inside the box, but the effort went over.After going ahead, Sony tried to surge in pressure to get back on level terms, but Sofapaka still had the chances. With 10 minutes remaining till halftime, Kevin Kimani saw his spectacular effort with a half volley from inside the box well collected by the keeper.On the other end, the pair of Yema Mwana and George Abege tried but in vain to get an effort on target.Sofapaka started the second half with the same tempo they had in the first and barely a minute in, Dayo came close with a shot from Kimani’s cut back but it was deflected for a corner.Sony Sugar’s David Simiyu vies for the ball with teh Sofapaka FC duo of Humphrey Okoti and Rodgers Aloro during a Kenyan Premier League match at the Ruaraka COmplex on April 15, 2018. PHOTO/Raymond MakhayaThe hosts were handed a massive advantage eight minutes into the second half when Samuel Olare was shown a straight red card after elbowing Mousa Omar jostling for space in the wall.With the one man advantage, Sofapaka piled pressure on the visitors and they came close with Kimani’s shot from a Dayo pass brushing off a Sony leg for a corner while on the hour mark, Stephen Waruru’s left foot volley was saved by keeper Omondi.The sugar millers had a brilliant chance to gather a point especially with a man down when the ball fell graciously on David Simiyu’s path one on one with keeper Kigonya, but he took a rushed decision for a shot that went wide.They were almost punished seven minutes later but Kimani’s effort after a quick change of passes with Dayo inside the box went wide.Simiyu however made amends for his miss earlier on scoring from the penalty spot with 14 minutes left on the clock after a defensive mix up in the Sofapaka box ended up in Humphrey Okoti handling the ball.0Shares0000(Visited 2 times, 1 visits today)
0Shares0000Kisumu All Stars players celebrate a goal in a past KPL match. PHOTO/Kisumu All Stars/TwitterNAIROBI, Kenya, Nov 9 – Kariobangi Sharks defender Amani Kyata turned the ball into his won net in the 89th minute to gift Kisumu All Stars their maiden Kenyan premier League victory with a 1-0 win in Kisumu on Saturday.In eight matches, All Stars had only picked up three points from three draws and were second from bottom of the pile, but the victory over the dull Sharks ensured they added a W to their statistics to move to 16th in the standings. Sharks meanwhile continued with their slump in form and dropped back to 15th in the log after losing their third match in four outings to increase the pressure on head coach William Muluya.Meanwhile, Tusker FC needed a stoppage time penalty to play to a 1-1 draw with KCB at the Afraha Stadium in Nakuru to move two points clear on top of the standings.Timothy Otieno stepped up to the pressure cooker to slot home in added time after a handball inside the box, cancelling out Reegan Otieno’s earlier goal.The bankers had to play almost one hour of the match with a man less after defender Bethwell Warambo was sent off midway through the second half after a second yellow card.The victory saw Tusker move to 17 points, two ahead of Gor Mahia and AFC Leopards who clash tomorrow in the Mashemeji Derby while KCB remained fourth with 15 points as well but an inferior goal difference.Posta Rangers meanwhile moved to fifth in the standings after a 3-0 thrashing of Chemelil Sugar in Narok.Charles Odette and Francis Nambute scored to give the mailmen a comfortable 2-0 half time lead before skipper Joseph Mbugi converted a penalty six minutes after the restart to seal the win.0Shares0000(Visited 13 times, 1 visits today)
Toni Caravaca – remember the name!The 12-year-old, on the books of Barcelona, looks to have a huge future in the game judging by this sensational goal.Playing in a ‘Mini El Clasico’ against Real Madrid, the tiny midfielder lined up a free-kick from more than 30 yards out and barely looked capable of lifting the ball off the ground.But he left the crowd stunned when he unleashed an unstoppable dipping drive into the back of Real’s net.
Gardai who stopped a van found 14 people inside including nine children – none of whom were wearing seat belts.Inspector David Kelly told Letterkenny District Court that Gardai stopped a Transit van at College Road on February 17th, 2011.The van was being driven by mum-of-three Margaret McDonagh, 27, of 109 Meadowbank, Letterkenny. She told Gardai that she was returning from a family wedding and was giving a number of people a lift home.Solicitor Patsy Gallagher told the court that there was no question of speed and that Mrs McDonagh was being very careful.He also said she had not been drinking at the wedding.However Judge Paul Kelly said he took a serious view of the situation considering none of the people under seventeen years of age were wearing safety belts.“The biggest problem here is the risk to the children. She took a serious risk in that someone could have run into the back of her and caused a serious injury,” he said.He fined Mrs McDonagh €100 for allowing a person under seventeen years of age to be driven without a seat belt and took all other charges into consideration.Follow us on www.twitter.com/donegaldailyFollow us on www.facebook.com/donegaldailySell anything on www.donegaldailyclassifieds.comGARDAI LEFT SHOCKED AFTER FINDING FOURTEEN IN VAN – NINE WITHOUT SEATBELTS! was last modified: November 2nd, 2011 by StephenShare 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:donegaldaily.comGardailetterkennyseatbelts
Watch every goal England scored at the 2018 World Cup NO JOY Lopetegui was axed on Wednesday, just TWO DAYS before Spain’s World Cup campaign begins against Portugal, with former captain Fernando Hierro taking his place.The move has stunned the footballing world, but Barcelona legend and World Cup winner Xavi believes the head of the Spanish Football Federation, Luis Rubiales, was left with little choice but to dispense with Lopetegui’s services following the way in which he handled his post-tournament deal with Real Madrid.Rubiales was furious at being told Lopetegui had agreed to take the Real job only five minutes before it was made public on Tuesday afternoon, two days before the World Cup kicks off.“It was not the right moment for Lopetegui to do what he did,” said Xavi.“It was hasty, untimely and unnecessary.” Paul Pogba buys France World Cup winners specially designed rings Why does Luis Suarez kiss his wrist when he celebrates a goal? “I believe Luis Rubiales did the right thing and was looking out on behalf of the FA.“The FA and the national team should be above any one person and whilst this was not the easy decision to make, it was the right one.“All these players will have been through similar situations to this before but I do not believe it will stop them from enjoying a strong World Cup.”Rubiales has fumed at Real Madrid’s underhand tactics when he announced Lopetegui’s departure in a press conference on Wednesday, saying their actions have jeopardised Spain’s chances of winning a second World Cup. diamond geezer Learn the words for England’s catchy Gareth Southgate song LU BEAUTY Fallon d’Floor World Cup latest on talkSPORT.com ‘It could have been me’ – Allardyce admits World Cup was tough to watch Xavi has slammed Real Madrid and Julen Lopetegui Arsenal star Laurent Koscielny admits he didn’t want France to win World Cup 2 2 misery SUPERSTITION A reminder to Liverpool fans about the very comical threat Neymar offers You’re the one Dele Alli reveals pre-match rituals and lucky charms he has before matches Xavi has BACKED the remarkable decision to sack Julen Lopetegui as Spain manager on the eve of the World Cup, and has taken a swipe at Real Madrid for throwing the national team’s preparations into disarray. Good times Julen Lopetegui left Spain just 24 hours before the start of the World Cup Lopetegui, unbeaten in 20 games as Spain boss, had signed a new contract with the national side just three weeks ago.“There are decisions we had to make, based on how you behave and on ethics,” Spain FA chief Rubiales said.“The national team belongs to everyone and we have to send a clear message to all employees that there is a way to behave and a way not to.“If it had been up to Julen I wouldn’t have found out five minutes beforehand.“You can’t do things this way, two days before the World Cup. We have been compelled to make this decision.”
The young man killed in an early morning car crash yesterday has been named as Jonathan ‘Johnny’ Doherty.The late Johnny Doherty.Originally from Stranacorkragh in Derrybeg but living in Falcarragh, Mr Doherty was killed when the car he was driving crashed into a ditch at Termon on the N56 around 7am.The 25 year old father-of-two was killed instantly at the scene and his passenger was taken to Letterkenny General Hospital but is not understood to have suffered life-threatening injuries. Gardai have launched a full investigation into the single car collision.It is understood the men’s car struck an electricity pole and knocked out power in the area.The road was immediately closed off and diversions were put in place as scene of accident investigators try to determine he cause of the crash.The victim was living with his finance and their two children in Falcarragh. Garda Superintendent David Kelly appealed for anyone who may have seen Mr Doherty’s silver BMW car in the Termon area at the time of the crash to contact them.Local county councillor Michael McBride said once again two families had been left devastated by a fatality on Donegal’s roads.“We have to always remember at times like these that two families have been left to pick up the pieces.“The loss of life is sad at any time but for a young man to lose his life is even more difficult. The thoughts and the prayers of the local community are with both families at this time,” he said. TRAGIC YOUNG MAN KILLED IN TERMON CRASH WAS FATHER-OF-TWO was last modified: September 9th, 2015 by StephenShare 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:crashderrybegdonegalFalcarraghJohnny DohertykilledTermon
SANTA CLARA – What’s in store for the next 49ers vs. Green Bay Packers fall classic? Our Week 12 mailbag, as compiled from input off my Instagram and Twitter feeds:Kittle! When?? Is the fact that he sat in a box last Sunday rather than standing in civvies on the sideline mean anything? (@Anthony04315169)Coach Kyle Shanahan said Kittle was assigned luxury-suite detail so he could stay off his injured leg and not stand on the sideline for three-plus hours. Unlike the Seattle game, Kittle came …
One of the biggest mysteries remaining in cell biology is how proteins fold. Proteins start out as chains of amino acids (polypeptides) as they exit the ribosome. Most of them spontaneously fold into their “native” three-dimensional structures, where they will go to work as enzymes, structural materials or other key players in cell life. About 10% of them are so complex, they need a little help. The GroEL+GroES enzymes act like a barrel-shaped dressing room to help these proteins escape the bustle of the cytoplasm so that they can fold in private. New work published in Cell shows that this “chaperone” device speeds up the proper folding of the polypeptide when it otherwise might get stuck on a “kinetic trap.”1 A German team likened the assistance to narrowing the entropic funnel. “The capacity to rescue proteins from such folding traps may explain the uniquely essential role of chaperonin cages within the cellular chaperone network,” they said. GroEL+GroES therefore “rescues” protein that otherwise might misfold and cause damage to the cell. The GroEL barrel and its GroES cap spend 7 ATP energy molecules opening and closing. The process can work in reverse, taking a misfolded protein and unfolding it as well. It might take several rounds for a complex protein to reach its native fold. These chaperonins operate in bacteria as well as higher organisms – and they are not the only chaperones. “Bacterial cells generally contain multiple, partly redundant chaperone systems that function in preventing the aggregation of newly synthesized and stress-denatured proteins,” the authors said. “In contrast to all other components of this chaperone network, the chaperonin, GroEL, and its cofactor, GroES, are uniquely essential, forming a specialized nano-compartment for single protein molecules to fold in isolation.” This fact has been known since the 1990s. Chakraborty et al focused on the ability of GroEL+GroES to rescue proteins from kinetic traps. Like a stack of six-sided rings, GroEL forms a barrel-shaped container. “Each subunit of GroEL is composed of an equatorial ATPase domain, an apical domain, and an intermediate hinge domain,” they explained. “The apical domains form the flexible ring opening and expose hydrophobic amino acid residues toward the central cavity for the binding of non-native substrate proteins.” GroES forms a cap or lid over this barrel, allowing the polypeptide inside to fold in isolation. The dressing room is large enough to fold proteins 60,000 atomic mass units in size. What is becoming clear is that the barrel is not just a passive container. It actually accelerates folding: “an active mechanism in promoting folding appears to operate in addition, based on the demonstration that GroEL/ES can substantially enhance the rate of folding for proteins,” increasing the folding rate by as much as 10-fold. Whether iterative cycles of folding and unfolding in the barrel cause the acceleration, or the isolation alone prevents kinetic traps, was not known. The team concluded that “protein confinement in the chaperonin cage has the capacity to reduce entropic folding barriers, thereby promoting the formation of native contacts.” If so, the entropic funnel picture is apt; a narrowing funnel prevents the protein from misfolding and guides it along the way to its correct shape. The team also helped confirm that a net negative charge on the interior of the barrel contributes to the accelerated folding. “These findings are consistent with recent theoretical considerations that the charged surface may induce ordered water structure, with the resulting increase in the density of water facilitating folding by enhancing the hydrophobic effect and thus promoting global protein compaction,” they said. This interior charge contribution only works when the protein is inside the barrel. Outside the barrel, they found that artificially induced disulfide bridges could coax their test polypeptide into the native fold. “In view of the fact that cells contain multiple, partially redundant chaperone systems for aggregation prevention, the ability to actively promote the folding of such intermediates would explain the uniquely essential role of the chaperonin cages,” they said in conclusion. On the other hand, the conspicuous absence of chaperonins from oxidizing cellular compartments correlates with the role of disulfide bond formation in providing an alternative mechanism to lower entropic folding barriers.” See also the 12/28/2007 entry, last two paragraphs. Meanwhile, scientists at Rice University have been trying to model protein folding on computers. PhysOrg quoted them saying that “Protein folding is regarded as one of the biggest unsolved problems in biophysics.” How proteins find their native fold through a maze of wrong folds is still not understood. “Like a river finding the shortest route to the sea, proteins always find their way to their native states in an instant,” the article said. “How that happens is one of life’s great mysteries.” Somehow they do it – and quickly. Many proteins spontaneously collapse into their proper shape in milliseconds or microseconds. “Though the proteins assemble themselves in nature almost instantly, the Rice team’s algorithm took weeks to run the simulation.” the article said. “Still, that was far faster than others have achieved.” Using another analogy to show what the protein (and simulators) are up against, one researcher said that “A polypeptide chain en route to its native state encounters many energy barriers, much like when one navigates through a rugged mountain landscape.” If you have supercomputers handy and weeks of free time, you might be able to run the Rice team’s new and improved simulation. The spontaneous folding of proteins vastly exceeds the complexity of human attempts at spontaneous origami (see New Scientist for primitive example). Once folded, proteins are workhorses in the cell, performing all kinds of intricate tasks. A recent article on PhysOrg, for instance, reported that scientists at the University of Dundee discovered an enzyme that acts like a “molecular scissors,” cutting off parts of DNA during damage repair operations. Some proteins incorporate metals into their structure. This adds to the difficulty of getting them into their native conformation, because they have to delicately position these highly reactive metal ions at precisely the right locations inside the fold. An article on PhysOrg did not address the folding problem per se, but marveled at these “hives of industry” in the cell, stating that “Nearly half of all enzymes require metals to function in catalysing biological reactions” such as photosynthesis, metabolism, and respiration. Kylie Vincent, of Oxford University’s Department of Chemistry, continued: “Both the metal and the surrounding protein are crucial in tuning the reactivity of metal catalytic centres in enzymes.” Oxford is keen on watching how metallic enzymes work in order to imitate them. “There is much that we can learn,” Kylie said, “from the way that micro-organisms use readily available metals to carry out these reactions while chemists often require rare and expensive metals for the same chemistry.” Clean, green fuel cells and other inventions may come from a better understanding of these amazing strings of amino acids that fold ever-so-precisely into the most efficient molecular machines ever witnessed.1. Chakraborty et al, “Chaperonin-Catalyzed Rescue of Kinetically Trapped States in Protein Folding,” Cell Volume 142, Issue 1, 112-122, 9 July 2010, DOI: 10.1016/j.cell.2010.05.027.None of these articles said anything about evolution. Why would natural selection produce a multi-part precision folding machine like GroEL+GroES, able to fold multiple different polypeptides, when other chaperone mechanisms exist? (cf. 12/30/2002). This is not clumsy tinkering; it is elegant extravagance showing the power of goal-directed design, utilizing an irreducibly complex machine (see 11/30/2006, bullet 7). One can envision Charlie worrying about this and spontaneously folding into a fetal position in his isolation chamber (tomb), never to come out again. It’s overkill by this point, but to rub it in, you might read Robert Deyes’ review Uncommon Descent of Doug Axe’s new paper, “The Case Against A Darwinian Origin Of Protein Folds,” available for open access in the new journal, Bio-complexity. Deyes titled his review, “Proteins Fold as Darwin Crumbles.”(Visited 15 times, 1 visits today)FacebookTwitterPinterestSave分享0