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Dynamics of Chains as a Tool to Study Thermomechanical Properties of Proteins.

Polymer dynamics can be formulated on different levels of detail. One approach eliminates microscopic degrees of freedom and a polymer molecule is represented by a simplified structure—a chain. In the simplest case monomers of ideal chain have fixed length, and their orientation is independent of the orientations and positions of neighbouring monomers. This is reason that two monomers can co-exist at the same place. Ideal chain model doesn’t describe correctly the local structure of polymer, but correctly describe the property on large-scale. In this scale chain can be treated as a thermodynamical system, which their dynamic have to fulfill laws of nonequilibrium thermodynamics. In a living systems there are a special polymers-proteins, that can operate under non-equilibrium conditions. During biochemical processes, they changes its states and are treated as free energy transducers. I will present a certain formalism of non-equilibrium thermodynamic when non-Markovian processes appear.

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Additional information

DOI
Digital Object Identifier link open in new tab 10.1007/978-3-030-77310-6
Category
Publikacja monograficzna
Type
rozdział, artykuł w książce - dziele zbiorowym /podręczniku w języku o zasięgu międzynarodowym
Language
angielski
Publication year
2021

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