Just as a single sheet of paper can be folded into a variety of different shapes, so can proteins.

Just as a single sheet of paper can be folded into a variety of different shapes, so can proteins. The correct folding of a protein is crucial to its proper functioning, and the cell uses a variety of chaperone molecules to help ensure correct protein folding. Researchers at Texas A&M University used a technique known as cryo-electron microscopy to figure out how a molecular chaperone called HSP60 turned a protein from a 2D string of amino acids into a 3D protein. HSP60 recognizes non-folded proteins and places them in a molecular "box" where it works with other molecules to fold the protein. The scientists published their results in the journal Cell. Protein misfolding causes proteins to aggregate in large clumps, which has been linked to Alzheimer's disease, amyotrophic lateral sclerosis (ALS, also known as Lou Gehrig's disease), and other neurological diseases. Understanding how protein misfolding goes wrong could help researchers better understand these illnesses.

Source: http://www.cell.com/abstract/S0092-8674(13)00528-X