There are hundreds of thousands of proteins for which amino acid sequence data are available, but whose structure and function remain unknown.

Now a research team, led by University of Illinois biochemistry professor John A. Gerlt, has devised a method to use a computational approach to accurately predict a protein’s function from its amino acid sequence. Their “in silico” (computer-aided) predictions were validated in the laboratory by means of enzyme assays and X-ray crystallography.

The new approach involved searching databases of known proteins for those with amino acid sequences that had the greatest homology to the unknown proteins.

When a cell is seriously stressed, say by a heart attack, stroke or cancer, a protein called Bak just may set it up for suicide, researchers have found.

In a deadly double whammy, Bak helps chop the finger-like filament shape of the cell’s powerhouse, or mitochondrion, into vulnerable little spheres. Another protein Bax then pokes countless holes in those spheres, spilling their pro-death contents into the cell.

“We found out Bak has a distinct function in regulation of the mitochondrial morphology,” says Dr. Zheng Dong, cell biologist at the Medical College of Georgia and the Veterans Affairs Medical Center in Augusta .

By bypassing a well-known gene implicated in almost one-third of all cancers and instead focusing on the protein activated by the gene, Dr. Christopher Counter and colleagues at the Duke University Medical Center have identified IL6 as a new target in the battle against Ras-induced cancers.

The ras gene, known as an oncogene when it is in this mutated state, has been implicated in several different cancers, including those of the pancreas and lungs. To date, efforts at blocking or turning off ras have proven ineffective.

To protect us from disease our immune system employs macrophages, cells that roam our body in search of disease-causing bacteria. With the help of long tentacle-like protrusions, macrophages can catch suspicious particles, pull them towards their cell bodies, internalise and destroy them.

Using a special microscopy technique, researchers from the European Molecular Biology Laboratory (EMBL) now for the first time tracked the dynamic behaviour of these tentacles in three dimensions. In the current online issue of PNAS they describe a molecular mechanism that likely underlies the tentacle movement and that could influence the design of new nanotechnologies.

Contrary to textbook models, many genes that should be 'off' in embryonic stem cells and specialized adult cells remain primed to produce master regulatory proteins, leaving those cells vulnerable to identity changes

Biologists have long thought that a simple on/off switch controls most genes in human cells. Flip the switch and a cell starts or stops producing a particular protein. But new evidence suggests that this model is too simple and that our genes are more ready for action than previously thought.

Scientists in the lab of Whitehead Member Richard Young have discovered that many human genes hover between “on” and “off” in any given cell. According to the study, these genes begin making RNA templates for proteins—a process termed transcription—but fail to finish.

ESA’s Venus Express and NASA’s MESSENGER looked at Venus in tandem for a few hours in June. Here is the first set of images.

The orbital geometry of Venus Express when MESSENGER skimmed past Venus on 5 June meant that the two spacecraft were not at the same location (with respect to the surface of the planet) at the exact same time. So how could they make true joint observations of the same regions and phenomena? Scientists came up with a highly creative solution.