“When we announced Withings Move in January, we received overwhelmingly positive feedback from consumers excited to have an activity tracker option that allows them to express themselves and showcase their personal style,” said Eric Carreel, Withings’ president, in a release. “We are thrilled to start shipping the watch that brings this combination of fashion and technology to a new level and soon offering even more design and customization options to our customers.”The watch is water-resistant to 50 meters, measures steps and sleep, and has a battery life of up to 18 months. The customization isn’t available for the $130 electrocardiogram (ECG or EKG) version of the watch, since that isn’t out yet. It’s likely to launch in a range of colors, then add custom options later, the spokesperson said.Withings returned to the ownership of co-founder Carreel last May, following Nokia’s decision to sell off the company.First published April 2 at 5:48 a.m. PT.Updated April 3 at 5:25 a.m. PT: Adds details about US shipping. 1:10 Wearable Tech 0 Now playing: Watch this: Share your voice Withings is letting Europeans customize their Move watches. Withings Withings has added a bunch of customization options for its Move fitness watch, but only on its European store for now.The watch, which the company revealed at CES in January, is available in five standard colors — black and yellow gold, white and coral, white and sea blue, black and mint, and white with black and mint — for $70 and started shipping in the US on Wednesday.European buyers can pay a little more to tweak the dial, case, strap and second hand color to their liking, and they can check out how it’ll look on the local versions of Withings’ site. In the UK, the price jumps from £60 ($78) to £70 ($91) for the custom style.The option will come to the US later this year, the French health technology company said in an emailed statement. Post a comment Tags Withings adds ECG to its newest watches and blood pressure…
Rahul Dravid and Sourav Ganguly enjoyed some great success together during their playing days. ReutersFormer Indian skipper Sourav Ganguly took to twitter and slammed the Board of Control for Cricket in India (BCCI) after they sent a conflict of interest notice to former cricketer Rahul Dravid. Ganguly stated that this new fashion of Indian cricket can hamper its future.”New fashion in indian cricket …..conflict of interest ….Best way to remain in news …god help indian cricket ……Dravid Gets Conflict of Interest Notice from BCCI,” his tweet read.Indian spinning legend Harbajhan Singh also criticised BCCI for these kinds of actions. He also mentioned that sending notices to these legends is like insulting them.”Really ?? Don’t know where it’s heading to.. u can’t get better person than him for Indian cricket. Sending notice to these legends is like insulting them.. cricket need their services for betterment. Yes god save indian cricket,” his tweet read. File photo of India off-spinner Harbhajan Singh.MAL FAIRCLOUGH/AFP/Getty ImagesRahul Dravid is currently the head of National Cricket Academy (NCA) in Bangalore. He got a notice from BCCI’s Ombudsman-cum-Ethics Officer Justice (Retd) DK Jain as a complaint was filed against the former claiming that Dravid, who is the NCA director currently, is also the vice-president of India Cements group. The complainant is a Madhya Pradesh Cricket Association (MPCA) life member Sanjeev Gupta. He had earlier complained against the likes of Sachin Tendulkar, Sourav Ganguly and VVS Laxman.A senior BCCI official on August 7 confirmed that Dravid has been sent a notice, according to IANS.”Yes, Dravid had been sent a notice by Jain last week and has two weeks to reply to the notice,” the official told IANS.But according to reports Dravid and India Cements had mutually decided to stall their association till the time the 46-year-old is the director of NCA.Because of this issue of the BCCI, many former players are refraining from applying for the posts at NCA. The Cricket Advisory Committee (CAC) members had to declare about any conflict before their appointment took place.
For the fragments that contain stable hydrophobic contacts (which cause the protein to fold), the protein/computer enforces these contacts and adds more residues to enlarge these points. If new hydrophobic contacts are formed again, the process continues until no more contacts are found.“The protein doesn’t ‘know’ it has the right starting points at the early stages,” Dill explained. “It explores many possible avenues. But, we find that when the chain pieces have reached roughly the 16-to-24-mer stage, then the differences in free energy begin to become compelling, and structures begin to emerge fairly clearly.”In some cases, this zipping procedure alone is enough for a protein to reach its native form. For other cases, the ZA algorithm switches to the assembly procedure, combining two or more fragments to form additional structures until the native form is achieved. The ZA method was tested on nine small proteins, eight of which closely matched the experimental results of samples in the Protein Data Bank. The greatest sign that the ZA method is on the right track is its speed. For example, using ZA, protein G could fold in about 1 CPU year on a 2.8-Ghz Xeon Intel machine.“We don’t know exactly what the speed gain is,” Dill said. “Our largest protein studied is a 112-mer (subsequent to the PNAS paper). Currently the most extensive all-atom physical simulations on Folding@Home, with 100,000 processors, or IBM’s Blue Gene, built for this problem, are on smaller proteins, typically in the range of 20-40 amino acids long. However, those simulations are also more directed at physical questions of folding, rather than at protein structure prediction, so it’s hard to make a direct comparison.”Citation: Ozkan, S. Banu, Wu, G. Albert, Chodera, John D., and Dill, Ken A. “Protein folding by zipping and assembly.” Proceedings of the National Academy of Sciences, July 17, 2007, vol. 104, no. 29, 11987-11992.Copyright 2007 PhysOrg.com. All rights reserved. This material may not be published, broadcast, rewritten or redistributed in whole or part without the express written permission of PhysOrg.com. Citation: Divide-and-conquer strategy key to fast protein folding (2007, August 6) retrieved 18 August 2019 from https://phys.org/news/2007-08-divide-and-conquer-strategy-key-fast-protein.html Researchers have found that proteins may use a divide-and-conquer strategy to fold into their native states in mere microseconds. The physical strategy, called “zipping and assembly” (ZA), can increase the speed at which supercomputers predict protein folding structures, greatly increasing scientists’ understanding of these building blocks of life. Explore further Ribbon diagrams of nine protein structures: Protein Data Bank structures are in orange, while Zipping & Assembly structures are in blue. Credit: Ozkan, et al. ©2007 PNAS. The scientists, Banu Ozkan, Albert Wu, John Chodera, and Ken Dill from the University of California at San Francisco, have published their research in a recent issue of the Proceedings of the National Academy of Sciences. Their results show that the ZA search strategy provides a physics-based model of protein folding that could lead to advances such as computer-based drug discovery and genetic engineering.“Our research has two significant points, I believe,” Dill told PhysOrg.com. “First, it shows that all-atom physical force fields are pretty good (but not perfect), and may be useful for protein structure prediction. And second, it proves that zipping and assembly is a highly efficient conformational search method, and supports the view that ZA may be the physical mechanism of protein folding.”Proteins, which consist of an unstructured linear chain of amino acids, can fold into complex 3D structures within microseconds. On the other hand, high-speed supercomputers might take tens of years to compute the correct structure due to the vast assortment of possible forms the protein could take. When folded incorrectly, proteins can cause neurodegenerative diseases such as Alzheimer’s and mad cow disease. How proteins fold so quickly is a mystery that researchers are approaching from many different angles, including, for example, physics-based force fields. By assigning force fields to different parts of the protein, computers can track the movement of each individual part.Using the ZA strategy, Ozkan, Wu, Chodera and Dill have sped up the rate at which computers using force fields can predict protein structures. In the ZA model, the first step that proteins (or computers) take is breaking the amino acid chain into 8-12 fragments to search for a very small fraction of favorable folding points (traditional methods usually search the entire chain).“The speed gain in our method comes from not exploring all possible folding routes, but instead from following only those routes that entail small conformational search steps,” Dill explained. “This reduces the search problem, in principle, from one that grows exponentially with the chain length to one that, instead, grows only as the first or second power of the chain length. While we haven’t actually proven that quantitatively, it is clear that the method is much faster than brute force Monte Carlo or molecular dynamics.” Parsley and dill help fight cancer, research shows This document is subject to copyright. Apart from any fair dealing for the purpose of private study or research, no part may be reproduced without the written permission. The content is provided for information purposes only.
This document is subject to copyright. Apart from any fair dealing for the purpose of private study or research, no part may be reproduced without the written permission. The content is provided for information purposes only. New dating of Neanderthal remains from Vindija Cave finds them older than thought Artifacts from the Anzick site. Credit: Texas A&M University © 2018 Phys.org Journal information: Proceedings of the National Academy of Sciences The Anzick site in Montana. The white post signals where the burial was found. Credit: PNAS Lorena Becerra-Valdivia at the Oxford Radiocarbon Accelerator Unit (ORAU), University of Oxford, working on the equipment (HPLC) that was used to extract hydroxyproline from the Anzick site bone samples. Credit: Eileen Jacob (University of Oxford, Oxford). Explore further More information: Lorena Becerra-Valdivia et al. Reassessing the chronology of the archaeological site of Anzick, Proceedings of the National Academy of Sciences (2018). DOI: 10.1073/pnas.1803624115AbstractFound in 1968, the archaeological site of Anzick, Montana, contains the only known Clovis burial. Here, the partial remains of a male infant, Anzick-1, were found in association with a Clovis assemblage of over 100 lithic and osseous artifacts—all red-stained with ochre. The incomplete, unstained cranium of an unassociated, geologically younger individual, Anzick-2, was also recovered. Previous chronometric work has shown an age difference between Anzick-1 and the Clovis assemblage (represented by dates from two antler rod samples). This discrepancy has led to much speculation, with some discounting Anzick-1 as Clovis. To resolve this issue, we present the results of a comprehensive radiocarbon dating program that utilized different pretreatment methods on osseous material from the site. Through this comparative approach, we obtained a robust chronometric dataset that suggests that Anzick-1 is temporally coeval with the dated antler rods. This implies that the individual is indeed temporally associated with the Clovis assemblage. Artifacts from the Anzick site. Credit: Texas A&M University In 1968, construction workers came upon the remains of an infant skeleton. Those remains became known as Anzick-1 and were believed to represent a member of the Clovis people. The Clovis people are believed to have been the first widespread group of people living in North America. Prior research has suggested they lived approximately 13,000 to 12,600 years ago. Their name comes from the distinctive Clovis-style projectiles they created.In the years after Anzick-1 was found, teams of researchers studying the remains found mixed results when testing for age. Some showed the remains as very nearly the same age as nearby Clovis artifacts, while others found the remains to be thousands of years more recent. In this new effort, the researchers sought to settle the matter once and for all using new and improved dating techniques.The new techniques involved using pretreatments of collagen found in the remains to factor out decontamination and for extracting a single amino acid for radiocarbon dating. The researchers report that all of their tests showed that antlers found near the burial site and the skull of a second specimen (Anzick-2) were roughly the same age—which was approximately the same as prior testing had shown. But some of the testing showed the remains of Anzick-1 to be approximately 1000 years younger. Another test the team performed, though, called HYP extraction, showed the infant remains to be approximately the same age as the antlers and Anzick-2. The differing results from the other tests, the researchers suggest, were likely due to contamination issues. They contend that because HYP is the more precise measurement technique, their results show that Anzick-1 is approximately the same age as the other artifacts. And this, they claim, suggests that the debate about the age of the remains should be considered resolved. A team of researchers from the University of Oxford, Texas A&M University and Stafford Research LLC has found evidence bolstering the theory that the skeletal remains of an infant unearthed in Montana are those of the only known Clovis burial. In their paper published in Proceedings of the National Academy of Sciences, the group describes their testing methods and what they found. Citation: New testing method suggests baby Anzick-1 was same age as surrounding Clovis artifacts (2018, June 19) retrieved 18 August 2019 from https://phys.org/news/2018-06-method-baby-anzick-age-clovis.html Lorena Becerra-Valdivia at the Oxford Radiocarbon Accelerator Unit (ORAU), University of Oxford, working on the equipment (HPLC) that was used to extract hydroxyproline from the Anzick site bone samples. Credit: Eileen Jacob (University of Oxford, Oxford).