He won the 2017 ATP Indian Wells Masters title. ?->(Show Answer!)

1. He won the 2017 ATP Indian Wells Masters title.

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MCQ->[u]News Item Dated 22 Jan 2017:[/u] Saina Nehwal's Triumph at Malaysia Masters FinalDays after recovering from knee injury during Rio Olympics, Saina Nehwal is back with a bang as this Indian badminton ace thrashes Pompawee Chochuwong of Thailand by 22-20 and 22-20, thereby claiming the Malaysia Masters Grand title.Quashing the air about her ability to win titles, the world No 10 Nehwal clinched her first Masters within five months since knee injury. Nehwal had to undergo surgery after an early exit from the Rio Olympics where her fellow citizen PV Sindhu created history by claiming the first silver medal for Indian badminton.Silencing the critiques, Saina returned to action within a quarter of her surgery setback. Once the absolute queen of Indian badminton, she faced early exits and missed the qualification mark for Sharjah World Super Series Finals. Also, she lost to Sindhu in the Premier Badminton League. However, Malaysia Masters Grand title has been her winning start to 2017.....

MCQ->Two completely penetrating wells are located L (in metres) apart, in homogeneous confined aquifer. The drawdown measured at the mid point between the two wells (at a distance of 0.5 L from both the wells) is 2.0 m when only the first well is being pumped at the steady rate of Q1 m3/sec. When both the wells are being pumped at identical steady rate of Q2 m3/sec, the drawdown measured at the same location is 8, 0 m. It may be assumed that the drawdown at the wells always remains at 10.0 m when being pumped and the radius of influence is larger than 0.5 L Q1/Q2 is equal to....

MCQ->He won the 2017 ATP Indian Wells Masters title.....

MCQ->Who has won the 2017 ATP Indian Wells Masters title?....

MCQ-> Cells are the ultimate multi-taskers: they can switch on genes and carry out their orders, talk to each other, divide in two, and much more, all at the same time. But they couldn’t do any of these tricks without a power source to generate movement. The inside of a cell bustles with more traffic than Delhi roads, and, like all vehicles, the cell’s moving parts need engines. Physicists and biologists have looked ‘under the hood’ of the cell and laid out the nuts and bolts of molecular engines.The ability of such engines to convert chemical energy into motion is the envy nanotechnology researchers looking for ways to power molecule-sized devices. Medical researchers also want to understand how these engines work. Because these molecules are essential for cell division, scientists hope to shut down the rampant growth of cancer cells by deactivating certain motors. Improving motor-driven transport in nerve cells may also be helpful for treating diseases such as Alzheimer’s, Parkinson’s or ALS, also known as Lou Gehrig’s disease.We wouldn’t make it far in life without motor proteins. Our muscles wouldn’t contract. We couldn’t grow, because the growth process requires cells to duplicate their machinery and pull the copies apart. And our genes would be silent without the services of messenger RNA, which carries genetic instructions over to the cell’s protein-making factories. The movements that make these cellular activities possible occur along a complex network of threadlike fibers, or polymers, along which bundles of molecules travel like trams. The engines that power the cell’s freight are three families of proteins, called myosin, kinesin and dynein. For fuel, these proteins burn molecules of ATP, which cells make when they break down the carbohydrates and fats from the foods we eat. The energy from burning ATP causes changes in the proteins’ shape that allow them to heave themselves along the polymer track. The results are impressive: In one second, these molecules can travel between 50 and 100 times their own diameter. If a car with a five-foot-wide engine were as efficient, it would travel 170 to 340 kilometres per hour.Ronald Vale, a researcher at the Howard Hughes Medical Institute and the University of California at San Francisco, and Ronald Milligan of the Scripps Research Institute have realized a long-awaited goal by reconstructing the process by which myosin and kinesin move, almost down to the atom. The dynein motor, on the other hand, is still poorly understood. Myosin molecules, best known for their role in muscle contraction, form chains that lie between filaments of another protein called actin. Each myosin molecule has a tiny head that pokes out from the chain like oars from a canoe. Just as rowers propel their boat by stroking their oars through the water, the myosin molecules stick their heads into the actin and hoist themselves forward along the filament. While myosin moves along in short strokes, its cousin kinesin walks steadily along a different type of filament called a microtubule. Instead of using a projecting head as a lever, kinesin walks on two ‘legs’. Based on these differences, researchers used to think that myosin and kinesin were virtually unrelated. But newly discovered similarities in the motors’ ATP-processing machinery now suggest that they share a common ancestor — molecule. At this point, scientists can only speculate as to what type of primitive cell-like structure this ancestor occupied as it learned to burn ATP and use the energy to change shape. “We’ll never really know, because we can’t dig up the remains of ancient proteins, but that was probably a big evolutionary leap,” says Vale.On a slightly larger scale, loner cells like sperm or infectious bacteria are prime movers that resolutely push their way through to other cells. As L. Mahadevan and Paul Matsudaira of the Massachusetts Institute of Technology explain, the engines in this case are springs or ratchets that are clusters of molecules, rather than single proteins like myosin and kinesin. Researchers don’t yet fully understand these engines’ fueling process or the details of how they move, but the result is a force to be reckoned with. For example, one such engine is a spring-like stalk connecting a single-celled organism called a vorticellid to the leaf fragment it calls home. When exposed to calcium, the spring contracts, yanking the vorticellid down at speeds approaching three inches (eight centimetres) per second.Springs like this are coiled bundles of filaments that expand or contract in response to chemical cues. A wave of positively charged calcium ions, for example, neutralizes the negative charges that keep the filaments extended. Some sperm use spring-like engines made of actin filaments to shoot out a barb that penetrates the layers that surround an egg. And certain viruses use a similar apparatus to shoot their DNA into the host’s cell. Ratchets are also useful for moving whole cells, including some other sperm and pathogens. These engines are filaments that simply grow at one end, attracting chemical building blocks from nearby. Because the other end is anchored in place, the growing end pushes against any barrier that gets in its way.Both springs and ratchets are made up of small units that each move just slightly, but collectively produce a powerful movement. Ultimately, Mahadevan and Matsudaira hope to better understand just how these particles create an effect that seems to be so much more than the sum of its parts. Might such an understanding provide inspiration for ways to power artificial nano-sized devices in the future? “The short answer is absolutely,” says Mahadevan. “Biology has had a lot more time to evolve enormous richness in design for different organisms. Hopefully, studying these structures will not only improve our understanding of the biological world, it will also enable us to copy them, take apart their components and recreate them for other purpose.”According to the author, research on the power source of movement in cells can contribute to
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