Siri co-founder talks to iMore about the future of technology, mobile interfaces, and implementing Siri
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Google itself may have thrown the pricing situation out of whack by offering up a contract-free GSM version of Samsung's Galaxy Nexus for just $399, but those adhering to Sprint's plans can't make use of that, anyway. The other CDMA / LTE-infused Galaxy Nexus is now shipping from Sprint, several months ahead of its first LTE rollout. $199.99 on a two-year contract nets you a device, while you can snag one for $549.99 sans any strings. It's also available in stores nationwide for those who'd prefer to try before they buy, and yes, Sprint users who activate a Google Wallet account within a week of activation will receive a $10 instant credit and an additional $40 within three weeks. Just try to ignore that Galaxy S III that'll launch next month, okay? (It's not a pure Google device, anyway.)
PSA: Sprint's LTE-infused Galaxy Nexus now available online and in stores originally appeared on Engadget on Wed, 25 Apr 2012 17:59:00 EDT. Please see our terms for use of feeds.
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Welcome to?Just Show Me on?Tecca TV, where we show you some tips and tricks for getting the most out of the?gadgets in your life. In today's episode we'll show you how to take pictures out of your?Photo Stream. If you don't want to let an unwanted picture clutter up your Photo Stream, there's no reason to leave it in place. Getting it out is easy!
For even more episodes of Just Show Me,?check out all our Just Show Me episodes. If you have any topics you'd like to see us cover, just drop us a line in the comments.
This article originally appeared on Tecca
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ScienceDaily (Apr. 23, 2012) ? Tiny pores, or channels, embedded in cell membranes are critical to the healthy functioning of cells. Charged atoms, or ions, move through these channels to generate the electrical signals that allow cells to communicate with one another.
New research at Washington University School of Medicine in St. Louis unveils some of the inner workings of certain channels involved in regulating electrical signals in nerve cells, relaxing muscle cells and "tuning" hair cells in the inner ear.
In a report published April 22 in the advance online edition of the journal Nature, the scientists have shown how an unusual protein -- one lacking any definable structure -- plays a key role in temporarily blocking the movement of ions through these channels after a cell fires off an electrical signal. Preventing ions from moving through the channel is important because it gives cells time to recharge so that they can continue firing.
The researchers studied large potassium channels, called BK channels, which allow potassium ions to move in and out of cells. Looking at the channels gave the Washington University researchers an opportunity to see how so-called intrinsically disordered proteins can operate in cells.
They found that an intrinsically disordered protein was responsible for inactivating the BK channel. These proteins are of particular interest to scientists because they defy the long-held notion that a protein's precise 3-dimensional form determines its function.
Lingle, a professor of anesthesiology and of neurobiology, and his colleagues monitored the electrical activity of BK channels as they opened and closed. Despite the disordered nature of the unstructured protein that closes the channel, the researchers found that it nestles into a receptor inside the BK channel in a highly specific way. This lock-and-key mechanism is essential to closing, or inactivating, the channel.
"It's a two-step process, which distinguishes it from most other inactivation mechanisms that have been described," Lingle says. "My guess is that the part of the protein that binds to the potassium channel receptor may have to move through some very narrow spaces. It may be that by having a less-defined structure, the protein can navigate more easily through tight spaces and to get to the binding site."
Lingle and his colleagues are currently attempting to study how the channels behave in mouse cells to learn more about the physiological effects of BK channel behavior.
Problems in regulating BK channels are known to be involved in epilepsy, asthma and cardiovascular disease. A better understanding of the way those channels operate might help scientists think about new ways to treat these conditions and determine why the disordered protein domains that regulate these channels don't have a well-defined structure.
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The above story is reprinted from materials provided by Washington University School of Medicine. The original article was written by Jim Dryden.
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