Modeling the Structure of Myoglobin within the Abelian Higgs Model

Моделирование структуры миоглобина в рамках абелевой модели Хиггса
S. D. Liubimov, N. V. Gerasimeniuk, A. A. Korneev, A. V. Molochkov
2025-11-14

heterogeneous external electric fieldinverse field reconstructionlattice Abelian Higgs modelmyoglobin modelingprotein tertiary structure
The analysis of multi-atomic systems from the first principles is highly computationally intensive, therefore it requires the finding of integral degrees of freedom. We propose the usage of the lattice Abelian Higgs model for the study of protein structure and dynamics. At the first step we have introduced heterogeneous external electric field in this model and have shown how this field affected the tertiary protein structure. At the second step we found the form of external field corresponding to native protein structure with experimental accuracy. We believe that this approach will allow one to model protein dynamics depending on external conditions.
1
An external field configuration reproducing the native myoglobin structure was determined with experimental accuracy.
2
Introducing a heterogeneous external electric field into the model alters tertiary protein structure, demonstrating field-dependent structural effects.
3
The approach promises modeling of protein dynamics under varying external conditions, potentially reducing computational cost compared to first-principles methods.
4
The lattice Abelian Higgs model can be used to study protein structure and dynamics as an integral-degree-of-freedom representation for multi-atomic systems.

Myoglobin protein modeled within the lattice Abelian Higgs model

Influence and determination of heterogeneous external electric fields on tertiary protein structure and finding field configurations that reproduce the native structure with experimental accuracy

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2025-11-14
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S. D. Liubimov
N. V. Gerasimeniuk
A. A. Korneev
A. V. Molochkov
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