So, someone tell me, did I miss it? Where is WCG mentioned in the article?

The mere existence of chaperone complex's sort of undermines Radford's misfolding work (first post). Proteins often have several relaxed (inert) states, and are often activated to go to work, through many different biochemical means. I wonder if Redfords group assessed for degradation. Single cell organism research is not always a good paradigm for the human body. It is highly unlikely that studying the folding route of one protein in a bug will lead to a cure for Schizophrenia or Parkinsons disease. Most of us have heard miracle break through a bit too often. It seems every science team now tries to justify its research with some sort of vague link to some disease.
Might have been nice if sciencedaily had elaborated on 'device'!
That papers title is, The mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints.

Researches are using the supercomputer "Anton" to simulate protein folding. For one of the proteins studied, they performed a 100-microsecond simulation and found the domain folds and unfolds the same way each time. Anton was built solely for the purpose of molecular dynamics simulations of the behavior of large biological molecules. The full article is available in Chemical and Engineering News.

The following image compares protein folding results from X-ray crystallography (blue) and Anton's simulations (red).

http://arstechnica.com/science/news/2011/02/x...us-as-it-vaporizes-it.ars

X-ray laser finds structure of a single virus as it vaporizes it

In two Letters in Nature, scientists are reporting that they have been able to reconstruct the structures of biological molecules using femtosecond X-ray pulses. In the first Letter, they imaged nano-crystals of the photosystem I protein, part of the photosynthetic machinery. In the second, they were able to image individual single mimiviruses, part of a family of giant viruses. We seem to be well on the way to single molecule structural imaging. [...] higher energy x-rays and shorter bursts are expected to increase resolution and decrease the size of the sample particles. Plans are already in the works for x-ray lasers 105 times brighter but with pulses lasting less than 10fs.

http://www.sciencecodex.com/polarized_microsc...how_proteins_are_arranged

Polarized microscopy technique shows new details of how proteins are arranged

[...] "Our new technique allows us to measure how components of large protein complexes are arranged in relation to one another," [...] there is a "resolution gap" between the two techniques primarily used to visualize protein complexes. Electron microscopy can reveal the broad outlines of a large protein complex, but it can't show details. X-ray crystallography, meanwhile, can show minute detail but only of a small piece of the complex; it can't say how the individual pieces fit together. To further complicate matters, both techniques require fixed samples – while they can give you an idea of what something looks like at a moment in time, they can't tell you how its pieces might move. [...] After genetically attaching fluorescent markers to individual components of the nuclear pore complex, the scientists replaced the cell's own copy of the gene that encodes the protein with the new form that has the fluorescent tag. Then, they used customized microscopes to measure the orientation of the waves of light the fluorescently tagged proteins emitted. By combining these measurements with known data about the structure of the complex, the scientists can confirm or deny the accuracy of previously suggested models. [...] Eventually, the scientists say their technique could go even further. Because the proteins' fluorescence can be measured while the cells are still alive, it could give scientists new insights into how protein complexes react to varying environmental conditions, and how their configurations change over time. [...]