2013/08/14 by Fabio Pichierri, Pichierri, Fabio
Biochemistry, Genetics and Molecular Biology · Materials Science · #Enzyme Structure and Function #Microtubule and mitosis dynamics #Photosynthetic Processes and Mechanisms #q-bio.BM
paper · pdf · doi:10.48550/arxiv.1308.3032
8 pages, 2 figures
arxiv created 2013/08/14 · arxiv updated 2013/08/15
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°. 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.