Document Type

Article

Publication Date

5-2014

Publication Title

Journal of Theoretical and Computational Chemistry

Volume

13

Issue

3

Publisher

World Scientific Publishing

Abstract

A large fraction of proteins function as homodimers, but it is not always clear why the dimerization is important for functionality since frequently each monomer possesses a distinctive active site. Recent work (PLoS Computational Biology, 9(2), e1002924) indicates that homodimerization may be important for forming an electrostatic funnel in the spermine synthase homodimer which guides changed substrates toward the active centers. This prompted us to investigate the electrostatic properties of a large set of homodimeric proteins and resulted in an observation that in a vast majority of the cases the dimerization indeed results in specific electrostatic features, although not necessarily in an electrostatic funnel. It is demonstrated that the electrostatic dipole moment of the dimer is predominantly perpendicular to the axis connecting the centers of the mass of the monomers. In addition, the surface points with highest potential are located in the proximity of the interfacial plane of the homodimeric complexes. These findings indicate that frequently homodimerization provides specific electrostatic features needed for the function of proteins.

Comments

This manuscript has been published in the Journal of Theoretical and Computational Chemistry. Please find the published version here (note that a subscription is necessary to access this version):

http://www.worldscientific.com/doi/abs/10.1142/S0219633614400070

World Scientific Publishing holds the copyright in this article.

Download

Share

COinS