The technique, which Hecht developed over the last 10 years and validated in experiments to be published in November, could prove useful in a wide range of fields. Custom-designed proteins, for example, could become a source of new drugs or could form the basis of new materials that mimic the strength and resilience of natural substances.

The range of proteins present in nature, while great, has evolved only as far as the needs of biological organisms, said Hecht. "Why should we be limited by a mere few million proteins?" he said. "We can now not only ask what already exists in the biological world, but go beyond that and ask what might be possible."

Everett Lipman, a new assistant professor of physics at the University of California, Santa Barbara, recently co-authored an article in the journal Science, describing an innovative study of how to "see" proteins as they fold, the result of experiments performed with co-workers at the National Institutes of Health.

The machinery of life arises from interactions between protein molecules, whose functions depend on the three-dimensional shapes into which they fold, said Lipman. Although proteins are composed of just 20 different building blocks (the amino acids), the process by which a given sequence of these components adopts its unique structure is complex and poorly understood. Folding proteins are too small to view with a microscope, so the researchers used a method called Forster Resonance Energy Transfer, or FRET, to study them. Using a microfabricated silicon device and a microfluidic mixing technique, they were able to observe single protein molecules at various times after folding was triggered.

According to the researchers, their findings point the way to studies that could begin to clarify the factors that determine whether a prion specific to cattle that causes bovine spongiform encephalopathy (BSE), or mad cow disease, might become infectious to humans.

The studies also suggest a new approach for treating disorders such as Alzheimer's disease that involve aberrant protein folding, said the researchers. It might be possible to develop drugs that would influence toxic proteins that aggregate into brain-clogging plaque to fold into less toxic versions, they said.

The work, presented in the Aug. 29 edition of Science, marks the first time protein-folding kinetics has been monitored on the single-molecule level. Proteins are long chains of amino acids. Like shoelaces, they loop about each other or fold in a variety of ways, and only one way allows the protein to function properly. Just as a knotted shoelace can be a problem, a misfolded protein can do serious damage. Many diseases, such as Alzheimer's, cystic fibrosis, mad cow disease and many cancers result from misfolded protein.

“We believe this is a new force in nature,” said Ariel Fernández, a Visiting Scholar in the Institute for Biophysical Dynamics. “It’s never been properly characterized before and it seems to be at the core of biological phenomena when examined at the nanoscale.”

"We believe this is a new force in nature," said Ariel Fernandez, a Visiting Scholar at the University of Chicago's Institute for Biophysical Dynamics. "It's never been properly characterized before and it seems to be at the core of biological phenomena when examined at the nanoscale."

Fernandez and Ridgway Scott, Professor in Computer Science and Mathematics at the University of Chicago, will announce the discovery in the July 4 issue of Physical Review Letters. The study combines proteomics-the computational approach to the study of proteins-with physical chemistry, which delves into the effect of chemical structure on physical properties.

Certain short amino acid chains, the building blocks of proteins, are capable of self-assembly into the disease-causing amyloid fibrils of Alzheimer's. Emory biochemistry professor David Lynn and his colleagues have now enticed these amyloid peptides to self-assemble into well-defined nanotubes 15 billionths of a meter across. Such nanotubes can now serve as minute scaffolds to build nanotechnological devices with potential applications in many fields. These findings are published in the May 21 issue of the Journal of the American Chemical Society in their paper "Exploiting Amyloid Fibril Lamination for Nanotube Self-Assembly."

Now, researchers at the University of Illinois at Urbana-Champaign have observed a protein that hit a speed limit when folding into its native state.

"Some of our proteins were folding as fast as they possibly could -- in only one or two microseconds," said Martin Gruebele, an Illinois professor of chemistry, physics and biophysics. A paper describing the work is to appear in the May 8 issue of the journal Nature.

Computational techniques alone may not provide all the answers, but they are powerful enough to have earned a place in the standard toolkit for protein research. The Sequence Alignment and Modeling System (SAM), introduced in the early 1990s by researchers at the University of California, Santa Cruz, has become one of the most popular software packages for the analysis of protein sequences.