A First Rigorous Attempt to Explain Charge Transport in a Protein-Ligand complex
From MaRDI portal
Publication:6424862
arXiv2301.13111MaRDI QIDQ6424862FDOQ6424862
Authors: Roisin Dempsey Braddell, Jone Uria-Albizuri, J.-B. Bru, S. Rodrigues 
Publication date: 5 January 2023
Abstract: Recent experimental evidence shows that when a protein (or peptide) binds to its ligand pair, the protein effectively "switches on" enabling long-range charge transport within the protein. Astonishingly, the protein-ligand complex exhibits conductances in the order of nanosiemens over distances of many nanometers and macroscopic Ohm's law emerges. Here, we investigate this emergent phenomenon via the framework of many-body (fermionic) quantum statistical principles. We propose a simple model which gives rise to an Ohm's law with vanishing quantum effects in its thermodynamic limit (with respect to length scales). Specifically, we consider protein-ligand complexes as a two-band 1D lattice Hamiltonian system in which charge carriers (electrons or holes) are assumed to be quasi-free. We investigate theoretically and numerically the behavior of the microscopic current densities with respect to varying voltage, temperature and length within reasonable physiological parameter ranges. We compute the current observable at each site of the protein-ligand lattice and demonstrate how the local microscopic charge transport behavior generates the macroscopic current. The overall framework contributes to the search for unifying principles for long-range charge transport and associated emergent laws in protein complexes, which is crucial for bioelectronics.
Mathematical biology in general (92B99) Statistical mechanics of nanostructures and nanoparticles (82D80) Applications of quantum theory to specific physical systems (81V99)
This page was built for publication: A First Rigorous Attempt to Explain Charge Transport in a Protein-Ligand complex
Report a bug (only for logged in users!)Click here to report a bug for this page (MaRDI item Q6424862)
