How hydrophobicity shapes the architecture of protein assemblies.

ABSTRACT: The interactions that give rise to protein self-assembly are basically electrical and hydrophobic in origin. The electrical interactions are approached in this study as the interaction between electrostatic dipoles originated by the asymmetric distribution of their charged amino acids. However, hydrophobicity is not easily derivable from basic physicochemical principles. Its treatment is carried out here considering a hydrophobic force field originated by "hydrophobic charges". These charges are indices obtained experimentally from the free energies of transferring amino acids from polar to hydrophobic media. Hydrophobic dipole moments are used here in a manner analogous to electric dipole moments, and an empirical expression of interaction energy between hydrophobic dipoles is derived. Th

SUBMITTER: Cedano JA 

PROVIDER: S-EPMC10371886 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature