Quantum integrable systems. Quantitative methods in biology

TL;DR

This paper explores quantum integrable systems using nonlinear integral equations and applies these methods to models like the Hubbard model, while also proposing an evolutionary algorithm model to simulate biological evolution and analyzing protein interface structures.

Contribution

It introduces a detailed formulation of quantum integrable models via the Baxter T-Q relation and develops an evolutionary model for biological processes, linking physics and biology.

Findings

Derivation of equations for specific integrable models

Analysis of infrared and ultraviolet limits

Insights into protein interface patterns

Abstract

Quantum integrable systems have very strong mathematical properties that allow an exact description of their energetic spectrum. From the Bethe equations, I formulate the Baxter "T-Q" relation, that is the starting point of two complementary approaches based on nonlinear integral equations. The first one is known as thermodynamic Bethe ansatz, the second one as Kl\"umper-Batchelor-Pearce-Destri- de Vega. I show the steps toward the derivation of the equations for some of the models concerned. I study the infrared and ultraviolet limits and discuss the numerical approach. Higher rank integrals of motion can be obtained, so gaining some control on the eigenvectors. After, I discuss the Hubbard model in relation to the N = 4 supersymmetric gauge theory. The Hubbard model describes hopping electrons on a lattice. In the second part, I present an evolutionary model based on Turing machines. The goal is to describe aspects of the real biological evolution, or Darwinism, by letting evolve populations of algorithms. Particularly, with this model one can study the mutual transformation of coding/non coding parts in a genome or the presence of an error threshold. The assembly of oligomeric proteins is an important phenomenon which interests the majority of proteins in a cell. I participated to the creation of the project "Gemini" which has for purpose the investigation of the structural data of the interfaces of such proteins. The objective is to differentiate the role of amino acids and determine the presence of patterns characterizing certain geometries.