Partition analysis of dipole moments in solution applied to functional groups in polypeptide motifs

Abstract

A partition analysis based on segments is developed for density functional theory defining solute dipole moments of functional groups, and the corresponding induced solvent dipoles representing solvent screening. The accuracy of dipoles from the fragment molecular orbital method is evaluated in comparison to unfragmented values. The analysis is applied to evaluate dipole moments of side chains, amino and carbonyl groups in common polypeptide motifs, α-helixes, β-turns, and random coils in solution. The membrane domain of the ATP synthase (1B9U) is analyzed, revealing the effect of the bend splitting of the α-helix into two pieces.