Protein aggregates can compromise the viability of affected cells.
How protein molecules engage in fatal attractions and entangling alliances is a key area of research for this year's Hans Neurath Lecturer. In this mode, two protein molecules interact by exchanging important functional sections. Eisenberg's current experiments are aimed at learning if 3-D domain swapping can account for pathogenic protein aggregates such as amyloids. Amyloid deposits are found in the brains of Alzheimer's victims and in the diabetic pancreas. These questions are a matter of growing practical importance as the human genome is being delineated.