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Forschungszentrum Jülich - Annual Report 2012

30 Forschungszentrum Jülich | Annual Report 2012 Faulty Folding – Catastrophic Consequences The doctor Alois Alzheimer, who was the first to describe the disease named after him more than 100 years ago, saw them under the microscope: clumped protein deposits in the brains of deceased individuals who had suffered from Alzheimer’s. To this day, researchers do not fully understand why protein molecules form insoluble structures referred to amyloid plaques that eventually cause the brain cells to die off. However, an important intermediate step in this process was observed with unprecedented precision by an international team of researchers headed by Dr. Philipp Neudecker from Forschungszentrum Jülich and Heinrich Heine University Düsseldorf. They published their findings in the renowned journal Science in April 2012. E very protein is born as a thread-like molecule in which amino acids are beaded together like a string of pearls. However, as soon as it is formed, the thread folds within seconds into a three-dimensional shape. This is by no means a matter of coincidence: the exact shape of the complete protein molecule is a decisive factor in it fulfilling its respective role as an enzyme, antibody, muscle fibre, or one of the many other functions of proteins in our body. Philipp Neudecker from the Institute of Complex Systems studied the folding process of a protein molecule required for signal transduction in