The use of Lennard-Jones potentials gives rise to an expected energy distribution for main-chain polypeptide conformations in the Ramachandran plot that matches well the observed distribution of phi, psi values in high-resolution proteins. The position of the energy minimum in the beta-strand conformation region is situated where there is a substantial contribution from the electrostatic attraction between the partial charge of the carbonyl carbon atom of one amino acid residue and that of the carbonyl oxygen atom of an adjacent residue. This attraction gives rise to a preference for the right-twisted beta-strand conformation compared with the left-twisted conformation. The majority of beta-sheets are twisted, almost always in one direction. Looking along a single strand, the twist is to the right. This twist also helps provide a rationale for the characteristic topology of the strand-helix-strand unit often observed in alpha/beta proteins. The electrostatic explanation for the twist we propose has not, to our knowledge, been explicitly suggested previously. The factor that has been most widely proposed to explain the twist is steric hindrance involving side-chain atoms. We provide evidence that the electrostatic effect is of comparable significance. Right-twisted beta-strands are geometrically closely related to polyproline II helices and to collagen helices, both of which are left-handed. Short regions of polyproline II type helices, which are sometimes, but not always, rich in proline residues, are common at protein surfaces. We point out that these helices are stabilised by the same carbonyl-carbonyl interactions as in right-twisted beta-strands.