Image courtesy of Oak Ridge National Laboratory
This is a visualization of drug molecules ("parade day-like balloons") in a simulated attack of the ribbon-like protein fibrils that are believed to be the cause of Alzheimer's disease.
Talk about some amazing origami. Imagine, if you can, taking a sheet of paper or two and folding them together with such tight precision that instead of creating a crane or a cat, you actually produce a working machine. Then imagine trying to do so while caught in the middle of a football crowd, being bumped and jostled from many directions.
Cells do this every second, assembling molecular machines known as proteins by folding long strings of amino acids. Proteins perform a variety of different functions, such as transmitting cellular signals and speeding essential chemical reactions.
That makes protein folding of great interest to scientists, especially since badly formed proteins might lead to diseases like Alzheimer's, Creutzfeldt-Jakob disease, Cystic Fibrosis and others. However, researchers have been unable to predict how proteins fold together with such precision, especially while being battered by fluid constantly moving inside cells.
That is until now. A team of researchers from the University of Pittsburgh and the Energy Department's Oak Ridge National Laboratory recently developed a computational technique that helps understand the process of protein folding. Specifically, the method, known as quasi-anharmonic analysis (QAA) provides insight into the intermediate steps that take place as a protein folds.
As in origami, certain folds are more important than others. Some may have little impact, while others will be critical in determining the final form (whether a bat or a hat or a crane or a cat). Better knowledge of protein folding could in turn provide more insight into the diseases associated with malformed proteins, as mentioned above, and potential fixes for those malformations. That in turn could lead to new possibilities for new treatments.
The team of researchers developed and improved their protein folding simulations, thanks to ORNL's first-class supercomputing facilities. Much of the data they checked the model against came from a technique known as neutron scattering. ORNL is the world's premiere center for neutron scattering research, thanks to its Spallation Neutron Source and High-Flux Isotope Reactor. ORNL researchers also search for insights in many related areas, such as modeling the mechanism of Alzheimer's disease at the molecular scale.
Inspiration and insight folding together with outstanding equipment to create the shape of a better future: Now that's amazing origami.
For more information on Oak Ridge National Laboratory, please go to: http://www.ornl.gov/. And for more information on DOE's Office of Science, please go to: http://science.energy.gov/.
Charles Rousseaux is a Senior Writer in the Office of Science.