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An improved, more stringent coil library C[sub (alpha)(beta)(t)](super intern) was introduced to extract the intrinsic conformational preferences of residues within a protein. It was found that these backbone preferences generate a statistical potential that accurately reproduces helical, beta-sheet, and polyproline II (PPII) propensities, which are often strongly affected, by the identity and conformation of the neighboring residues.

Basic local backbone motions in unfolded chains are identified by performing simulations on a variety of peptide systems by using three popular force fields and for implicit and explicit solvent models. The correlated motion is viewed as a rocking of the plane of the peptide group, which is found both for fluctuations within each Ramachandran basin and during transit between different basins.