On the orientation of the backbone dipoles in native folds.

ABSTRACT: The role of electrostatic interactions in determining the native fold of proteins has been investigated by analyzing the alignment of peptide bond dipole moments with the local electrostatic field generated by the rest of the molecule with and without solvent effects. This alignment was calculated for a set of 112 native proteins by using charges from a gas phase potential. Most of the peptide dipoles in this set of proteins are on average aligned with the electrostatic field. The dipole moments associated with alpha-helical conformations show the best alignment with the electrostatic field, followed by residues in beta-strand conformations. The dipole moments associated with other secondary structure elements are on average better aligned than in randomly generated conformations. The alig

SUBMITTER: Ripoll DR 

PROVIDER: S-EPMC1140453 | biostudies-literature | 2005 May

REPOSITORIES: biostudies-literature