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UNIVERSITY OF BUCHAREST
FACULTY OF PHYSICS Guest
2024-11-22 1:23 |
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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 and Claudia Gabriela Firanescu
Affiliation:
Department of Electricity and Biophysics, Faculty of Physics, University of Buchares
E-mail
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 spatially fold must be clarified in order to improve the prevention and treatment of certain diseases.
We are reminding some of the protein folding diseases: Alzheimer’s disease, Parkinson, Mad Cow, Creutzfeldt-Jacob, and some types of cancer.
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 chain’s state of minimum energy or the protein’s “native conformation”.
An increasing number of severe diseases are the result of the 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.
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