Diseases occur for many reasons, including bacteria, viruses, mutations, and incorrect protein folding. Proteins are among the most important molecules in biology as they are what perform or trigger a cellular process, and their operation is determined by both their chemical makeup and their structure. Diseases such as Alzheimer's, Parkinson's, and Huntington's are all the result of misfolded proteins, which is why researchers are trying to understand how proteins fold and those at the Max Planck Institute for Biophysical Chemistry have taken an impressive step towards that end.
A good way to satisfy one's curiosity about something is to watch it happen, but proteins are so small you cannot see them with a microscope. Also you have to be able to trigger protein folding while you are watching, and methods involving high temperatures and pressure can cause the folding to occur too rapidly to see. To trigger the folding, the Max Planck researchers decided to use low temperatures by cooling their sample from 25 ºC to -16 ºC and then used Nuclear Magnetic Resonance (NMR) spectroscopy to watch what happens.
The researchers found that as the protein, CylR2, was cooled it broke into two subunits which were stable, at first. As the temperature dropped further, these intermediate subunits become unstable and dynamic, which may then lead to the incorrect protein folding that causes disease.