F. Colonna-Cesari, S. Premilat
Jun 15, 1975
Citations
0
Influential Citations
12
Citations
Journal
Journal of molecular biology
Abstract
The β pleated sheet structures of poly-l-alanine and the polydipeptide (Ala-Gly)n are analysed by conformational energy calculations, and the results are compared with the structures previously determined by X-ray methods. Structural parameters calculated for β poly-l-alanine using two different sets of potentials are in close agreement (within 5% or less) with the results of X-ray structure analysis (Arnott et al., 1967). For (Ala-Gly)n, the alanyl and glycyl-glycyl intersheet distances calculated by assuming the model of Fraser et al. (1965) are comparable to those observed in the polydipeptide, but differ significantly from those of (Gly)n and (Ala)n. These calculations help establish the structural details of both the polydipeptide and the closely related Bombyx mori silk protein in their β form.