Finding low-energy conformations of lattice protein models by quantum annealing

TL;DR

This paper demonstrates the first implementation of lattice protein folding under the Miyazawa-Jernigan model using quantum annealing, showcasing potential for quantum approaches in biophysical optimization problems.

Contribution

It introduces a quantum annealing benchmark for protein folding models, including the first implementation on a quantum device for the MJ model.

Findings

Successfully implemented quantum annealing for protein folding on up to 81 qubits.

First quantum device application of the Miyazawa-Jernigan model.

Provides a pathway for quantum optimization in biophysics.

Abstract

Lattice protein folding models are a cornerstone of computational biophysics. Although these models are a coarse grained representation, they provide useful insight into the energy landscape of natural proteins. Finding low-energy three-dimensional structures is an intractable problem even in the simplest model, the Hydrophobic-Polar (HP) model. Exhaustive search of all possible global minima is limited to sequences in the tens of amino acids. Description of protein-like properties are more accurately described by generalized models, such as the one proposed by Miyazawa and Jernigan (MJ), which explicitly take into account the unique interactions among all 20 amino acids. There is theoretical and experimental evidence of the advantage of solving classical optimization problems using quantum annealing over its classical analogue (simulated annealing). In this report, we present a benchmark implementation of quantum annealing for a biophysical problem (six different experiments up to 81 superconducting quantum bits). Although the cases presented here can be solved in a classical computer, we present the first implementation of lattice protein folding on a quantum device under the Miyazawa-Jernigan model. This paves the way towards studying optimization problems in biophysics and statistical mechanics using quantum devices.