Dipole-dipole interactions in protein-protein complexes: a quantum mechanical study of the ubiquitin-Dsk2 complex

TL;DR

This study uses quantum mechanical calculations to analyze dipole-dipole interactions in the ubiquitin-Dsk2 protein complex, revealing how these interactions stabilize and orient the proteins during complex formation.

Contribution

It provides the first quantum mechanical insight into dipole interactions in this specific protein-protein complex, highlighting their role in stabilization and orientation.

Findings

Dipole moments are aligned in a head-to-tail configuration.

Dipole interactions stabilize the complex.

Interactions favor correct protein orientation.

Abstract

Quantum mechanical calculations are performed on the proteins that constitute the ubiquitin-Dsk2 complex whose atomic structure has been experimentally determined by NMR spectroscopy (PDB id 1WR1). The results indicate that the dipole moment vectors of the two proteins are aligned in a head-to-tail orientation while forming and angle of ~130{\deg}. Hence, attractive dipole-dipole interactions not only stabilize the protein-protein complex but they are likely to favor the correct orientation of the proteins during the formation of the complex.