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Molecular structure of many polymers creates elastic rigidity that
impacts polymers behavior. Understanding this impact is critical to
address the physics describing variety of single-molecule
experiments and biological processes. Utilizing analytical theories
and numerical methods, we illustrate the effect of molecular
elasticity on the behavior of single molecules employed in
single-molecule experiments as well as the morphology of
assemblages in protein self-assembly processes. In single-molecule
experiments, we address the effect of thermal fluctuation, focusing
on the equilibrium statistical behavior of specific class of
underling single molecules (semiflexible polymers) to gain insight
into the physics governing their behavior. To demonstrate the role
that molecular elasticity plays in protein self-assembly processes,
we focus on clathrin protein, a protein recruited by the cell wall
for ingesting food particles during endocytosis. We demonstrate
that molecular elasticity and binding affinity have a significant
impact on the versatile equilibrium and nonequilibrium assemblages
occurred in clathrin protein self-assembly process.
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