Proteomics News

Protein assassin

Saturday, February 25, 2012 00:00 MST

Scientists find that the unfolded end of a protein can kill E. coli-like bacteria selectively. The results, which will be presented at the 56th Annual Meeting of the Biophysical Society, may one day help scientists find new, more targeted ways to kill antibiotic-resistant microbes.

Mapping proteins key to human health and immune system

Tuesday, February 21, 2012 00:00 MST

Proteins, the building block for all living organisms, are the ultimate transformers -- able to splice and switch roles and functions within the human body. But when these changes go wrong, diseases such as cancers and arthritis may result, says University of British Columbia researcher Chris Overall.

Let's stretch...

Monday, February 20, 2012 00:00 MST

The proteins actin, myosin and titin are big players in the business of muscle contraction. Scientists at the European Molecular Biology Laboratory (EMBL) in Hamburg, Germany, have now examined another muscle protein -- myomesin -- which they discovered can stretch up to two-and-a-half times its length, unfolding in a way that was previously unknown. The study is published Feb. 14 in the open-access, online journal PLoS Biology.

Stretching helices help keep muscles together

Friday, February 17, 2012 00:00 MST

Scientists at EMBL Hamburg have discovered that the elastic part of myomesin, a protein that links muscle filaments, can stretch to two and a half times its original length, unfolding in a way that was hitherto unknown.

Protein libraries in a snap

Tuesday, February 14, 2012 00:00 MST

A Rice University undergraduate will depart with not only a degree but also a possible patent for his invention of an efficient way to create protein libraries, an important component of biomolecular research.

Protein structures give disease clues

Saturday, February 04, 2012 00:00 MST

Discoveries about the shape and structure of biological molecules could potentially lead to new ways to treat or prevent diseases such as breast cancer and Alzheimer's disease.

Detailed picture of how myoV 'walks' along actin tracks

Wednesday, February 01, 2012 00:00 MST

A new study in the Journal of General Physiology uses state-of-the-art fluorescence microscopy to provide a striking 3-D picture of how class V myosins (myoV) "walk" along their actin track.

The secret life of proteins

Monday, January 30, 2012 00:00 MST

Researchers have identified a new and unusual role for a key player in the human immune system. A protein initially believed to regulate one routine function within the cell has proven vital for another critical step in the activation of the immune system.

Scientists probe form, function of mysterious protein

Saturday, January 28, 2012 00:00 MST

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.

Under the electron microscope -- a 3-D image of an individual protein

Friday, January 27, 2012 00:00 MST

Berkeley Lab scientists are reporting the first 3-D images of an individual protein ever obtained with enough clarity to determine its structure.

Energy-saving chaperon Hsp90

Monday, January 16, 2012 00:00 MST

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.

Scientists paint new picture of dance between protein and binding partners

Thursday, January 12, 2012 00:00 MST

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.

Temperature, entropy and protein binding

Thursday, January 05, 2012 00:00 MST

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.

Faster, more accurate, more sensitive

Monday, January 02, 2012 00:00 MST

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.

Cell membrane proteins could provide targets for broader vaccines

Saturday, December 31, 2011 00:00 MST

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.