2026
2.
Andriy Goychuk
Gaussian closure and dynamical mean-field theory for self-avoiding heteropolymers Miscellaneous
2026, (Version Number: 1).
Abstract | Links | BibTeX | Tags: Mean Field Theory, Polymers, Soft Condensed Matter
@misc{goychuk_gaussian_2026,
title = {Gaussian closure and dynamical mean-field theory for self-avoiding heteropolymers},
author = {Andriy Goychuk},
url = {https://arxiv.org/abs/2604.02085},
doi = {10.48550/ARXIV.2604.02085},
year = {2026},
date = {2026-01-01},
urldate = {2026-05-29},
publisher = {arXiv},
abstract = {Analytical treatments of polymer dynamics have mostly been restricted to linear response theory around some steady state obtained via perturbative field theory. Here, I derive an analytical framework that yields unified access to the evolution of conformations, contact probabilities, and fluctuations within a dynamical mean-field theory. Starting with the Langevin equation of a hydrodynamically coupled and self-avoiding heteropolymer, the key idea is to focus on the two-point correlator as the lowest-order relevant observable. Truncating higher-order correlations via a Gaussian closure leads to a self-consistent diffusion equation for the chain correlations. The theory is validated by contrasting coiled, globular, and self-avoiding polymers within a single dynamical framework, and predicts hyper-compacted fractal states in hydrodynamically coupled active polymers such as chromatin.},
note = {Version Number: 1},
keywords = {Mean Field Theory, Polymers, Soft Condensed Matter},
pubstate = {published},
tppubtype = {misc}
}
Analytical treatments of polymer dynamics have mostly been restricted to linear response theory around some steady state obtained via perturbative field theory. Here, I derive an analytical framework that yields unified access to the evolution of conformations, contact probabilities, and fluctuations within a dynamical mean-field theory. Starting with the Langevin equation of a hydrodynamically coupled and self-avoiding heteropolymer, the key idea is to focus on the two-point correlator as the lowest-order relevant observable. Truncating higher-order correlations via a Gaussian closure leads to a self-consistent diffusion equation for the chain correlations. The theory is validated by contrasting coiled, globular, and self-avoiding polymers within a single dynamical framework, and predicts hyper-compacted fractal states in hydrodynamically coupled active polymers such as chromatin.
2019
1.
Andriy Goychuk; Erwin Frey
Protein Recruitment through Indirect Mechanochemical Interactions Journal Article
In: Physical Review Letters, vol. 123, no. 17, pp. 178101, 2019, ISSN: 0031-9007, 1079-7114.
Abstract | Links | BibTeX | Tags: Analytical Theory, Biomolecular Self-Assembly, Elastic Deformation, First Passage Problems, Mean Field Theory, Pattern Formation, Protein-Membrane Interactions, Protein-Protein Interactions
@article{goychuk_protein_2019,
title = {Protein Recruitment through Indirect Mechanochemical Interactions},
author = {Andriy Goychuk and Erwin Frey},
url = {https://link.aps.org/doi/10.1103/PhysRevLett.123.178101},
doi = {10.1103/PhysRevLett.123.178101},
issn = {0031-9007, 1079-7114},
year = {2019},
date = {2019-10-01},
urldate = {2026-05-29},
journal = {Physical Review Letters},
volume = {123},
number = {17},
pages = {178101},
abstract = {Some of the key proteins essential for important cellular processes are capable of recruiting other proteins from the cytosol to phospholipid membranes. The physical basis for this cooperativity of binding is, surprisingly, still unclear. Here, we suggest a general feedback mechanism that explains cooperativity through mechanochemical coupling mediated by the mechanical properties of phospholipid membranes. Our theory predicts that protein recruitment, and therefore also protein pattern formation, involves membrane deformation and is strongly affected by membrane composition.},
keywords = {Analytical Theory, Biomolecular Self-Assembly, Elastic Deformation, First Passage Problems, Mean Field Theory, Pattern Formation, Protein-Membrane Interactions, Protein-Protein Interactions},
pubstate = {published},
tppubtype = {article}
}
Some of the key proteins essential for important cellular processes are capable of recruiting other proteins from the cytosol to phospholipid membranes. The physical basis for this cooperativity of binding is, surprisingly, still unclear. Here, we suggest a general feedback mechanism that explains cooperativity through mechanochemical coupling mediated by the mechanical properties of phospholipid membranes. Our theory predicts that protein recruitment, and therefore also protein pattern formation, involves membrane deformation and is strongly affected by membrane composition.