Protein conformational dynamics and electronic structure

TL;DR

This study investigates how the conformational flexibility of ubiquitin influences its electronic properties, using quantum mechanical calculations on multiple conformers to reveal fluctuations in key electronic parameters.

Contribution

It provides the first detailed link between protein conformational dynamics and electronic structure through quantum calculations on numerous conformers.

Findings

HOF, dipole moment, HOMO/LUMO energies, and HOMO-LUMO gap fluctuate across conformers.

Electronic properties are sensitive to conformational changes.

The study establishes a connection between protein dynamics and electronic structure.

Abstract

Quantum mechanical calculations are performed on 116 conformers of the protein ubiquitin (Lange et al., Science 2008, 320, 1471-1475). The results indicate that the heat of formation (HOF), dipole moment, energy of the frontier orbitals HOMO and LUMO, and HOMO-LUMO gap fluctuate within their corresponding ranges. This study thus provides a link between the conformational dynamics of a protein and its electronic structure.