Proteomics Research and News
 | Using computer models and laboratory experiments, scientists from Rice University and the University of California, San Diego have probed the structure of the protein mitoNEET to better understand its role in aging, cancer and diabetes. They found the protein could untangle its arms at one end to loosen its grip on a potentially toxic molecule of iron and sulfur. Their research is described this week in the Proceedings of the National Academy of Sciences. ...> Full Article |
Berkeley Lab scientists are reporting the first 3-D images of an individual protein ever obtained with enough clarity to determine its structure.
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 | A special group of proteins, the so-called chaperons, helps other proteins to obtain their correct conformation. Until now scientists supposed that hydrolyzing ATP provides the energy for the large conformational changes of chaperon Hsp90. Now a research team from the Nanosystems Initiative Munich could prove that Hsp90 utilizes thermal fluctuations as the driving force for its conformational changes. The renowned journal PNAS reports on their findings. ...> Full Article |
 | Using a blend of technologies, scientists from the Florida campus of the Scripps Research Institute have painted a new picture of how biochemical information can be transmitted through the modification of a protein. Previously, scientists believed that during the pairing of proteins and their binding partners ("ligands"), proteins modified their shape while ligands remained stable. The new study shows this one-size-fits-all solution is not entirely accurate.
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The binding of proteins to substrates is essential for organic life. In the 54th issue of Science China, one paper investigates the relationship between environmental temperature and the capture radius for protein binding. It was found that the largest capture radius corresponds to the folding transition temperature of a protein chain. The results could provide valuable reference data for future research.
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Sequence comparisons are an essential tool for the prediction and analysis of the structure and functions of proteins. A new method developed by computational biologists at the LMU permits sequence comparisons to be performed faster and more accurately than ever before.
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Vaccines with broader reach might be made by stimulating specialized immune cells to recognize foreign cell membrane proteins that are shared across bacterial species, say researchers from Children's Hospital of Pittsburgh of UPMC and the University of Pittsburgh School of Medicine in a report published online today in Immunity. The approach could be particularly beneficial in preventing infection by multi-drug resistant organisms.
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A protein's function depends on both the chains of molecules it is made of and the way those chains are folded. And while figuring out the former is relatively easy, the latter represents a huge challenge with serious implications because many diseases are the result of misfolded proteins. Now, a team of chemists at the University of Pennsylvania has devised a way to watch proteins fold in "real-time," which could lead to a better understanding of protein folding and misfolding in general.
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CSHL scientists have discovered hydrogen sulfide -- the flammable, toxic gas associated with the smell of rotten eggs in landfills -- helps regulate a signaling pathway implicated in biological malfunctions linked to Alzheimer's and Parkinson's diseases, among others.
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 | With few exceptions, all known proteins are built up from only twenty amino acids. 25 years ago scientists discovered a 21st amino acid, selenocysteine and ten years ago a 22nd, the pyrrolysine. However, how the cell produces the unusual building block remained a mystery. Now researchers at the Technische Universitaet Muenchen have elucidated the structure of an important enzyme in the production of pyrrolysine. The scientific journal Angewandte Chemie reports on their results. ...> Full Article |
A team of Vanderbilt chemists have designed and successfully synthesized the largest artificial protein using a new approach that greatly expands scientists' ability to create proteins unknown in nature.
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Researchers from Hull, Bristol and Frankfurt have shown that a new technique for identifying molecular structure can be used effectively on small samples of biological proteins, particularly proteins that are targeted for drug development.
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Scientists at Rochester Institute of Technology and Dowling College are matching proteins to the job they perform in the human body. Their research could lead to drugs that target proteins and switch on or off specific functions associated with various diseases. The three-year study is funded by a grant from the National Institutes of Health's National Institute of General Medical Sciences.
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Researchers studying the nature of crowds playing Foldit called some strategies "shocking" in how well they mimicked some of the methods already used by protein scientists. In a paper published online at the Proceedings of the National Academy of Sciences, University of Washington researchers reveal the creative power of Foldit players' strategies and compare them to the best-known scientist-developed methods.
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 | Research led by St. Jude Children's Research Hospital scientists has identified an unexpected mechanism facilitating some protein interactions that are the workhorses of cells and, in the process, identified a potential new cancer drug development target. ...> Full Article |
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