RYAN POPPEAbbott Campaign Mail-in Ballot ApplicationGov. Greg Abbott’s campaign to register mail-in ballot applications for seniors ahead of the deadline is creating costly headaches for many county election officials. During a primary election season, campaigns will try to help senior citizens register for mail-in ballots. But Texas election officials, including Bexar County’s election administrator Jacquelyn Callanen, are mailing back hundreds of applications, all of them linked to one campaign.“When we receive a primary election, we receive a number of mail-in ballot applications from a number of campaigns and we started to receive some last week that did not have a party check on them,” Callanen said.Those incomplete applications came from Abbott’s re-election campaign and were mailed not only to seniors that voted Republican in the last election but also to traditional Democrat and independent voters, according to the campaign.Campaign spokesman John Wittman said part of its effort is to attract voters who don’t traditionally vote in a Republican primary.“This mail-in ballot application drive is result of a test that Texans for Greg Abbott did in 2014. This election, we’ve expanded it 10-fold,” Wittman said.Glen Maxey, who heads up the Texas Democratic Party’s mail-in ballot campaign, was one of the first to notice problems with the Abbott application, which he said is decorated with the Abbott campaign logo and has very small printed instructions informing the voter they must indicate whether they need a Democrat or Republican mail-in ballot.“This application is about six-point type. A person of age — such as myself — I can’t read the application even with my glasses,” Maxey said.Callanen said it is costing individual counties hundreds of dollars to reject the incomplete applications, and the extra effort of sending out all the rejection letters is slowing down her office’s productivity.The deadline to submit an application for a mail-in ballot is Feb. 23. Share
The Lambda Kappa Omega chapter of Alpha Kappa Alpha will hold their annual Kozy Kerchief & Kozy Kaps program at the Vienna Presbyterian Church, 124 Park St. NE, on Oct. 24 from 8 a.m. until 4 p.m. The event will take place on National Make A Difference Day and consist of AKA members and volunteers creating, sewing and hand delivering head wraps for women and children undergoing cancer treatments at local hospitals.For more information, visit aka-lko.org/programs/kozy-kerchief-kozy-kaps
(Phys.org)—A pair of researchers at Duke University has built a library of protein data that outlines the specific amino acid sequences that control changes of many elastin proteins. In their paper published in the journal Nature Materials, Felipe García Quiroz and Ashutosh Chilkoti describe their research, the making of their library, and their belief that what they have created will help in the development of new synthetic designs for possible use in medical applications. Citation: Researchers develop a library of elastin-like proteins to help in creating synthetic designs (2015, September 23) retrieved 18 August 2019 from https://phys.org/news/2015-09-library-elastin-like-proteins-synthetic.html Proteins assemble and disassemble on command 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. More information: Sequence heuristics to encode phase behaviour in intrinsically disordered protein polymers, Nature Materials (2015) DOI: 10.1038/nmat4418AbstractProteins and synthetic polymers that undergo aqueous phase transitions mediate self-assembly in nature and in man-made material systems. Yet little is known about how the phase behaviour of a protein is encoded in its amino acid sequence. Here, by synthesizing intrinsically disordered, repeat proteins to test motifs that we hypothesized would encode phase behaviour, we show that the proteins can be designed to exhibit tunable lower or upper critical solution temperature (LCST and UCST, respectively) transitions in physiological solutions. We also show that mutation of key residues at the repeat level abolishes phase behaviour or encodes an orthogonal transition. Furthermore, we provide heuristics to identify, at the proteome level, proteins that might exhibit phase behaviour and to design novel protein polymers consisting of biologically active peptide repeats that exhibit LCST or UCST transitions. These findings set the foundation for the prediction and encoding of phase behaviour at the sequence level. Journal information: Nature Materials © 2015 Phys.org Explore further Proteins are organic compounds essential to all living organisms, they are especially prevalent in components that have structure, such as muscle, skin, hair, etc. They provide structure by self-forming into different shapes under different conditions, two of which are solubility and temperature. Proteins are made of sequences of amino acids—the order and type of which drive the shape of the protein when certain conditions are met. Scientists still do not quite understand how proteins self assemble into the specific 3D shapes they take, nor which amino acids lead to which shapes, or indeed, how the order in which they exist contributes to those shapes. To help provide a better understanding of how it all works, Quiroz and Chilkoti set about building a library of all the known elastin-like proteins, along with the shapes they take under different conditions. They based it on the sequences of five key amino acids found in the fibrous protein typically found in connective tissue, such as muscles. They then set about testing each entry in the library by growing samples of E. coli engineered to produce proteins that folded into different shapes under different conditions. Most specifically noted was under which conditions the proteins shifted from being soluble to non-soluble and vice-versa. That work led them to developing a set of rules that loosely defined which amino acid sequences would result in which shapes under which conditions.The research duo acknowledge that their rules are more like guidelines, but suggest the basis of what they have built can not only be made stronger with more research by them and others, but can be used to assist in creating synthetic proteins for use in developing targeted drugs. One example would be protein capsules that remain insoluble inside the body until a certain condition is met, at which point, a medication would be released.