Civilian Ambassadors Forge Links between Grand Forks AFB Community

first_img Dan Cohen AUTHOR A group of civilian ambassadors appointed by the wing commander of Grand Forks Air Force Base has been staying busy, keeping the Grand Forks community in eastern North Dakota up to date about activities at the installation, organizing military appreciation day events and traveling to Washington to meet with Pentagon officials.“Having a close relationship between the community and the base is very important. We always want the community to know what we’re doing out here, so we’re not a mystery,” said Wing Commander Col. Paul Bauman, who has been at the installation for about two years.The ambassadors are briefed on Air Force and air base activities during at least one event annually, and are invited to attend events planned for visiting high-ranking military leaders and other important visitors, reported the Grand Forks Herald. There currently are eight base ambassadors.The base ambassador program is an outgrowth of the Grand Forks-East Grand Forks Chamber of Commerce Military Affairs Committee, and the ambassadors typically work with the committee on military appreciation day events. But Bauman drew a distinction with the community support groups that are active in most defense communities.“It’s unique,” he said. “One of the things that’s been interesting is feeling the closeness of the community to the base.”The tight connection between the installation and the community likely stems from the series of crises the two have been forced to cope with, including earlier BRAC rounds when the base was targeted for closure and the devastating flooding of the Red River in 1997.“A lot of that has forged close ties between the base and the community,” Bauman said. “Not every community has gone through that degree of trauma, so that adds to the uniqueness.”last_img read more

5 Things To Do In Wilmington On Saturday January 26 2019

first_imgWILMINGTON, MA — Below are 5 things to do in Wilmington on Saturday, January 26, 2019:#1) Wilmington Boosters Annual DanceThe Wilmington High School Boosters Association is holding its annual Dance at 7pm at the Tewksbury/Wilmington Elks Lodge (777 South Street, Tewksbury).  This fun evening includes live music from the local band WildFire.  Attendees are encouraged to bring their own food. Tickets cost $25 each and will be available at the door.#2) Suburban Boston Spring Home ShowThe Suburban Boston Spring Home Show will emanate from Wilmington’s  Shriners Auditorium (99 Fordham Road) on Friday, January 25 (11am-8pm); Saturday, January 26 (10am-8pm); and Sunday, January 27 (10am-6pm). Admission is $10 at the door. (Free passes are available online in advance HERE.) Parking is free. Learn more HERE.#3) Parent/Child Drawing 101 At LibraryThe Wilmington Memorial Library (175 Middlesex Avenue) is holding a drawing class for kids & adults from 9:30am to 11:30am. Join Gina Johnson, Co-founder & Portrait  Artist of “Operation: Home Ties “Faces of Remembrance”, for a beginners drawing class for children and the grownup of their choice. Share the amazement of learning to sketch using simple shapes. Gina believes there is an artist in each of us! Let her make a believer out of you with her fun step-by-step instructions – so you too will say: “Yes…I CAN draw”! Grades 1-5. Register HERE.#4) Book Store Next Door OpenThe Friends of the Wilmington Memorial Library’s Book Store Next Door (183 Middlesex Avenue) is open from 10am to 4pm. All books are $2 or less!  Every penny of every sale benefits the Wilmington Memorial Library. Learn more HERE.#5) Wilmington Food Pantry OpenThe Wilmington Food Pantry (142 Chestnut Street) is open from 10am to noon for food donation drop-offs. Learn which food items the Pantry is most in need of HERE.Like Wilmington Apple on Facebook. Follow Wilmington Apple on Twitter. Follow Wilmington Apple on Instagram. Subscribe to Wilmington Apple’s daily email newsletter HERE. Got a comment, question, photo, press release, or news tip? Email wilmingtonapple@gmail.com.Share this:TwitterFacebookLike this:Like Loading… Related5 Things To Do In Wilmington On Thursday, August 22, 2019In “5 Things To Do Today”5 Things To Do In Wilmington On Saturday, August 10, 2019In “5 Things To Do Today”The Wilmington Insider For January 27, 2018In “5 Things To Do Today”last_img read more

Hunt for Huntingtons cause yields clues

first_imghttp://news.rice.edu/files/2016/11/1114_POLYGLUTAMINE-1-WEB-1uwa05n.jpgRice University researchers built computer simulations of mutated proteins implicated in Huntington’s and other neurological diseases to see how they develop. From left, Weihua Zheng, Min-Yeh Tsai, Peter Wolynes and Mingchen Chen. (Credit: Jeff Fitlow/Rice University) AddThis http://news.rice.edu/files/2016/11/1114_POLYGLUTAMINE-2-web-1mf49zm.jpgA graphic shows the simulated aggregation of proteins implicated in Huntington’s and other neurological diseases. (Credit: Mingchen Chen/Rice University)Located on a 300-acre forested campus in Houston, Rice University is consistently ranked among the nation’s top 20 universities by U.S. News & World Report. Rice has highly respected schools of Architecture, Business, Continuing Studies, Engineering, Humanities, Music, Natural Sciences and Social Sciences and is home to the Baker Institute for Public Policy. With 3,910 undergraduates and 2,809 graduate students, Rice’s undergraduate student-to-faculty ratio is 6-to-1. Its residential college system builds close-knit communities and lifelong friendships, just one reason why Rice is ranked No. 1 for happiest students and for lots of race/class interaction by the Princeton Review. Rice is also rated as a best value among private universities by Kiplinger’s Personal Finance. To read “What they’re saying about Rice,” go to http://tinyurl.com/RiceUniversityoverview. https://youtu.be/9kk8rSiH3p8A simulation shows 20-repeat polyglutamines aggregating. These low-repeat proteins require four or more in close proximity to form a nucleus around which aggregates can form. (Credit: Wolynes Research Lab/Rice University) Share1Editor’s note: Links to videos and high-resolution images for download appear at the end of this release. David Ruth713-348-6327david@rice.eduMike Williams713-348-6728mikewilliams@rice.eduHunt for Huntington’s cause yields cluesRice University scientists analyze repeats in proteins implicated in neurological diseases HOUSTON – (Nov. 10, 2016) – Rice University scientists have uncovered new details about how a repeating nucleotide sequence in the gene for a mutant protein may trigger Huntington’s and other neurological diseases.Researchers at Rice’s Center for Theoretical Biological Physics used computer models to analyze proteins suspected of misfolding and forming plaques in the brains of patients with neurological diseases. Their simulations confirmed experimental results by other labs that showed the length of repeating polyglutamine sequences contained in proteins is critical to the onset of disease.The study led by Rice bioscientist Peter Wolynes appears in the Journal of the American Chemical Society.Glutamine is the amino acid coded for by the genomic trinucleotide CAG. Repeating glutamines, called polyglutamines, are normal in huntingtin proteins, but when the DNA is copied incorrectly, the repeating sequence of glutamines can become too long. The result can be diseases like Huntington’s or spinocerebellar ataxia.The number of repeats of glutamine can grow as the genetic code information is passed down through generations. That means a healthy parent whose huntingtin gene encodes proteins with 35 repeats may produce a child with 36 repeats. A person having the longer repeat is likely to develop Huntington’s disease.Aggregation in Huntington’s typically begins only when polyglutamine chains reach a critical length of 36 repeats. Studies have demonstrated that longer repeat chains can make the disease more severe and its onset earlier.The paper builds upon techniques used in an earlier study of amyloid beta proteins. That study was the lab’s first attempt to model the energy landscape of amyloid aggregation, which has been implicated in Alzheimer’s disease.This time, Wolynes and his team were interested in knowing how the varying length of repeats — as few as 20 and as many as 50 — influenced how aggregates form.“The final form of the protein detected in people who have Huntington’s disease is a macroscopic aggregate made of many molecules, much like an ice crystal formed out of water has many molecules in it,” Wolynes said. “This process needs to start somewhere, and that would be with a nucleus, the smallest-size cluster that will then be able to finish the process and grow to macroscopic size.“People knew that the length of the repeats is correlated with the severity of a disease, but we wanted to know why that matters to the critical nucleus size,” he said.Experiments had demonstrated that sequences of 20 repeats or less remained unfolded – or “noodle-y,” as Wolynes described them; they were able to clump into a nucleus only when four or more were gathered together in proximity.The researchers’ simulations showed how sequences with 30 repeats or more are able to fold by themselves without partners into hairpin shapes, which are the building blocks for troublesome aggregates. Thus, for the longer sequences, even a single protein can begin the aggregation process, especially at high concentrations.The Rice team found that at intermediate lengths between 20 and 30 repeats, polyglutamine sequences can choose between straight or hairpin configurations. While longer and shorter sequences form aligned fiber bundles, simulations showed intermediate sequences are more likely to form disordered, branched structures.“We don’t know if branching is good or bad,” Wolynes said. “But it explains the weird shapes the experimentalists get in the test tube.”Mutations that would encourage polyglutamine sequences to remain unfolded would raise the energy barrier to aggregation, they found. “What’s ironic is that while Huntington’s has been classified as a misfolding disease, it seems to happen because the protein, in the bad case of longer repeats, carries out an extra folding process that it wasn’t supposed to be doing,” Wolynes said.The team’s ongoing study is now looking at how the complete huntingtin protein, which contains parts in addition to the polyglutamine repeats, aggregates.Rice graduate student Mingchen Chen is lead author of the paper. Co-authors are Rice postdoctoral researcher Min-Yeh Tsai and research scientist Weihua Zheng. Wolynes is the D.R. Bullard-Welch Foundation Professor of Science, a professor of chemistry, of biochemistry and cell biology, of physics and astronomy and of materials science and nanoengineering at Rice and a senior investigator of the NSF-funded Center for Theoretical Biological Physics at Rice.The National Institute of General Medical Sciences and the Ministry of Science and Technology, Taiwan, supported the research. The researchers used the NSF-supported DAVinCI supercomputer administered by Rice’s Ken Kennedy Institute for Information Technology.-30-Read the abstract at http://pubs.acs.org/doi/abs/10.1021/jacs.6b08665Follow Rice News and Media Relations via Twitter @RiceUNewsVideos:center_img https://youtu.be/Zy_yEnPJNeoA simulation shows 30-repeat polyglutamines aggregating. These higher-repeat proteins require only one to nucleate aggregates of the type implicated in Huntington’s disease. (Credit: Wolynes Research Lab/Rice University) https://youtu.be/YlV3dCFIpZgA simulation shows 30-repeat polyglutamines aggregating in slow motion. (Credit: Wolynes Research Lab/Rice University)Related materials:Wolynes Research Lab: http://wolynes.rice.edu/node/129Center for Theoretical Biological Physics: https://ctbp.rice.eduWiess School of Natural Sciences: http://natsci.rice.eduImages for download: https://youtu.be/Jg1bfz9PKZw A simulation shows 20-repeat polyglutamines aggregating in slow motion. (Credit: Wolynes Research Lab/Rice University)last_img read more