Although biomimetic nanotechnology is in its infancy, with no applications yet reaching commercialization, the barriers in some cases lie mainly in scaling up production processes to industrial levels. In others, researchers must make significant basic breakthroughs to bridge the gap between laboratory experiments and usefulness.

Using lasers to initiate and probe the folding process, a group including chemist Timothy Zwier have precisely determined the energies needed to twist tryptamine, a molecule with several flexible "hinges" that bears a close resemblance to an amino acid, the basis of proteins. Understanding the energy pathways that these molecules take passing from one conformation to another could provide new understanding of the elusive process of protein folding - an essential part of the development of these fundamental biological molecules. And though tryptamine forms only a tiny portion of a protein, a better understanding of this close chemical relative to serotonin and melatonin could provide insights into these other substances' effect on the brain.

"If you want to know how molecules function in the body, you can't just look at their structure - you have to look at the dynamics of how they change," said Zwier, who is a professor of chemistry in Purdue's School of Science. "On a small scale, we have found a way to look at the dynamic processes that makes one such molecule change shape. While we're still a long way from understanding how proteins take on their complex shapes, this work could be a step in that direction."

"FamClash is quite successful at qualitatively predicting the pattern of the specific activity of the hybrids," the researchers report in this week’s online issue of the Proceedings of the National Academy of Sciences. "By identifying incompatible residue pairs in the hybrids, this method provides valuable insights for protein engineering interventions to remedy these clashes," the researchers say.

FamClash is a computer method used to predict which hybrid enzymes are likely to have activity and which are not. Hybrid enzymes form when researchers combine similar enzymes from two or more different organisms. The variant enzymes are broken and recombined with parts from the original enzymes creating the new one.

Prions (pronounced PREE-ons) are one of countless types of proteins found in normal cells, and are at the center of the mystery. Scientists, who identify proteins by their shapes and molecular structures, know the job descriptions of many of them: Some act like bricks in the structure of a cell, while others help cells carry out chemical reactions or communicate with other cells. Prions appear to be important since there are so many of them in our brain cells, but, like the boss' son-in-law, their role in the whole organization is unclear.

In fact, one British researcher found that genetically modified mice without prions look and act exactly the same as other mice. "You can't talk to a mouse, and maybe it's lacking in some function, but as far as (the researcher) could tell, the mouse was perfectly normal," said David Eisenberg, who studies prions at the University of California at Los Angeles.

As proteins form within cells, their long chains of amino acids fold up like fiendishly intricate origami. Since the 1930s, scientists have known that a protein's folded shape is key to its function, making it possible for hemoglobin to carry oxygen or for collagen to bind together skin. But figuring out how and why proteins fold the way they do has become one of the great, enduring challenges in biochemistry.

It's easy for proteins to get corrupted while folding in the crowded confines of a cell, and misfolded proteins can cause all sorts of trouble.

When the abnormal form comes into contact with normal transporter prions, the normal ones begin a chain-reaction of bizarre folding that ultimately leads to the destruction of neurologic tissue and death.

All proteins are simple chains of amino acids that coil into specific shapes to perform their biological function.

In the folding process, proteins are assisted by molecular chaperones that function to prevent misfolding or, in the case of already misfolded proteins, to detect them and prevent their accumulation.

Faulty proteins have been implicated in such neurodegenerative diseases as Huntington's, Parkinson's and Alzheimer's.

Morimoto and colleagues have shown that elevated levels of molecular chaperones promote longevity.

The researchers focused on a master protein called heat shock factor.

Now, after years of painstaking research, scientists have succeeded in duplicating the disease's most critical features in the most readily manipulated model organism in existence. In research published in this week's issue of the journal Science, a team from Whitehead Institute for Biomedical Research used common baker's yeast as a living test tube to show how just a small amount of a Parkinson's-related neuronal protein called alpha-synuclein (aSyn) can convince neighboring proteins to abandon their normal shape and form these deadly clusters.

"For the first time we can initiate the process synchronously in living cells and watch what is happening in real time," says Susan Lindquist, director of Whitehead Institute and a lead author of this new study.

A protein's shape is critical to its function: When a protein changes its shape, it changes function, and this can be deadly. Many neurodegenerative diseases such as Parkinson's are thought to be caused by proteins like aSyn that can misfold into abnormal shapes and lose their ability to function correctly or even wreak havoc in the cell.

So say two University of Florida scientists who have used the newly developed techniques of 'paleobiochemistry' to reconstruct ancient bacterial proteins based on similarities in the genetic sequences of modern proteins. The resurrected proteins proved most stable and functional at temperatures between 130 and 150 degrees Fahrenheit, implying that ancient bacteria lived in a hot springs-like soup warmer than most life can tolerate today.

For proteins, form really does equal function. Not only are they essential building blocks of the body, but proteins are also the workers of every cell, carrying out its specific functions. This function depends on the ultimate three-dimensional shape of the protein, a form achieved by folding flexible chains of amino acids until each is properly aligned so that the protein can do its job. Normally, the folding of proteins is highly efficient and specific, but sometimes the process goes awry, resulting in dangerous misfolded forms.