The main idea in the protein folding field is that the sequence of a protein determines the three dimensional shape a protein will assume once it is made. If the protein is purified from healthy animals and from sick animals and compared, it has the same sequence of amino acids, but a different shape. This is a highly unusual method of disease propagation that raises many questions. Indeed it hasn't been definitively proven yet, and people have been looking for a viral component for years. I'm proposing experiments to address looking at sequence elements that are important for the three dimensional structure of the protein, both its toxic and normal structure, especially I'd like to ask how much of the protein can be manipulated before it loses infectivity so those portions of it can be narrowed down for further study.
Protein folding is quite an up and coming field.
Since a protein is a linear sequence of amino acids stuck together like popcorn on a string that folds up into a particular shape, you might think of a piece of freshly cooked spaghetti and what it would look like if you dropped it on the floor. The slides at quite a few seminars these days show pictures that look alot like what you might see. The integrity of that squiggly curled up shape seems to be one of the key determinants to life and consciousness as we know it. The longer technical version.