UNIVERSITY OF BUCHAREST
FACULTY OF PHYSICS

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2024-11-24 23:02
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Conference: Bucharest University Faculty of Physics 2003 Meeting


Section: Electricity and Biophysics


Title:
Protein Folding. Diseases Caused by Misfolding


Authors:
Adriana Cristina Toma, Drd. Claudia Gabriela Firanescu


Affiliation:
Department of Electricity and Biophysics, Faculy of Physics, University of Bucharest


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Keywords:


Abstract:
What exactly is this phenomenon? We all learned that proteins are fundamental components of all living cells: our own, the bacteria that infect us, the plant and animals we eat. Given that proteins are present in all living systems, the function of proteins and how they fold must be clarified in order to improve the prevention and treatment of certain diseases. For every protein chain, there is theoretically some combination of twists, turns and bends that puts it in a minimum energy state - its most comfortable and stable position. The dominant strategy in solving the protein-folding problem has been to find an amino acid chains state of minimum energy or the proteins native conformation. An increasing number of severe diseases have been traced to protein misfolding and formation of insoluble aggregates. Common to many of these disorders is that certain proteins can adopt a non-native conformation that aggregates to form insoluble protein fibrils. Protein folding diseases can be divided into two groups: in the first, excessive quantities of wrongly folded proteins collect in the form of uncontrolled piles of molecular rubbish. This is the group of diseases known as amyloidoses, of which Alzheimer s disease is the best-known example. In the other, a small error in genetic blueprint leads to incomplete folding of a protein, which affects its function. This might, for instance, happen to the protein, p53. The malfunctioning of this central tumour suppressor could cause cancer. One of the main characteristics of Alzheimer s disease is the accumulation of plaques of insoluble ß-amyloid in the brain. The plaques are formed by cleavage of amyloid-precursor protein, which release amyloid-ß peptide fragments. These then form fibrils, which aggregate into insoluble clumps of ß-amyloid plaques that surround neurons and might cause damage.