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.

Research teams from universities in the US and Germany believe that certain arrangements of protein fibres could be produced reliably over and over again in an industrial setting.

These could be "coated" in gold or silver, potentially producing wires thousands of times smaller in diameter than the tiniest available currently.

RAPTOR (Rapid Protein Threading Predictor), a protein-structure-prediction
program developed on the university's SGI Origin 3800 supercomputer by
graduate student Jinbo Xu under the supervision of Professor Ming Li, was
ranked No.1 for fold recognition among non-meta programs by scientists
associated with the CAFASP competition.

The results hold implications for the study of the related "protein folding problem." Researchers are working to understand the issues nature has to overcome to design new RNA sequences, because someday researchers may be able to design sequences themselves, for drugs or other disease therapies.

Transthyretin is secreted by the liver into the bloodstream. It helps to circulate hormones and vitamins around the body.

The researchers, from the Scripps Research Institute in La Jolla, say specially designed small molecules can help prevent proteins from folding into shapes that lead to disease. Their work is described in today's issue of the journal Science.

Screening for several compounds, the scientists found that an anti-inflammatory drug prescribed for arthritis called diflunisal can stabilize the protein transthyretin.