Genetic Mutation And Disordered Protein Structure | 12175
Journal of Biotechnology & Biomaterials
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Intrinsically disordered proteins lack a stable structure and adopt many various conformations within a short time‐scale.
Genetic mutation impacts the structures and free energy landscapes of disordered proteins. The structure and function
relationship definition in medicine and biology, which states that the 3‐Dimensional structure of a protein defines its biological
function captures native state proteins without serious limitations, however, intrinsically disordered proteins do not possess
stable 3‐Dimensional structures and yet they have well defined biological functions. For more than two decades, researchers from
diverse fields have been trying to find a direct relationship between the structures and thermodynamic properties of intrinsically
disordered proteins. Various tools have been developed without providing a direct relationship between the disordered protein
structures and their thermodynamic properties, such as free energy. Most recently, we developed new theoretical strategies that
relate genetic mutation directly to disordered protein structures and conformational free energy surfaces. In this talk, we will
present these new strategies and their applications on genetic mutation and disordered proteins at the center of neurodegenerative diseases.
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