The protein folding process is one of the fundamental biological processes, whichsignificantly changes with age. The age-related pathological process leads to an uncontrolledproduction, reorientation, and storage of proteins in cells and tissues. These proteins aggregateto form fibrils. The protein fibrils often accumulate in the nerve system, being responsible forthe development of neurodegenerative disorders such as Alzheimer or Jacobs-Kraft disease. Itwas recently found that protein fibrils also accumulate in leaver, joints, kidneys, leading to thedevelopment of lethal diseases. In the last years, significant scientific attention is directed tothis challenging sociological problem. Due to large structural analogy to fibrils formed byamyloid protein, they are called amyloid fibrils. The scientific investigations aim at thedistinction between the synthesis, correct and pathological folding of proteins. Numerousstructure analyzing techniques are employed to study amyloid fibril structures. The structureof protein fibrils is known and displays large structural arrangement of a native correctlyfolded protein. However, the mechanism of their formation, dynamic structural changesleading to protein misfolding and aggregation remain unknown. Use of in situ states of the art bioanalytical complementary methods is required to identifystructural changes in the complex pathway of the protein misfolding process. Bothcooperation partners, aim at investigations of the protein misfolding process leading to theformation of amyloid fibrils.
