FRET, FRAP and speckle microscopy are a few quantitative imaging techniques that scientists use to measure direct molecular interactions inside cells. These data help decipher how cellular functions arise from many proteins acting together—something that cannot be understood merely by analyzing the details of individual molecules. Extracting this information efficiently from a stack of images has been enabled by high-throughput methods coupled with pattern recognition algorithms. These tools aid the construction of information pathways and macromolecular assembly models for understanding how proteins transition from one activity to another. An example of project in this area is shown below.
Nuclear Pore Complex and Multiscale Modeling
A collaborative research team succeeded in dissecting the structure of the nuclear pore complex (NPC), an assembly of 456 proteins that controls the flow of molecules between the nucleus and the rest of the cell. The video highlights 30 different types of proteins found in the donut-shaped complex from yeast. The work may shed light on the function and evolution of the NPC and other large protein assemblies. Credit: Andrej Sali, University of California, San Francisco; Michael Rout and Brian Chait, Rockefeller University. Video featured with permission from Macmillan Publishers Ltd: Nature 450:695-701, 2007. Article abstract 