Calibration of effective van der Waals atomic contact radii for proteins and peptides

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Abstract
Effective van der Waals radii were celebrated in such a way that molecular models built from standard bond lengths and bond angels reproduced the amino acid conformations observed by crystallography in proteins and peptides. The celebrations were based on the comparision of the Ramachandbran plots prepared from high-resolution X-ray data of protins and peptides with the allowed ϕ,ψ torsional angel space for the depeptide molecular models. The celebrated radii are useful as criteria with which to filter energetically improbable conformations in molecular modeling studies of proteins and peptides.