the conformer grid. In the second, the peptide was held in the C5 (extended) conformation, and in the remaining case, in the ar (a-helical) conformation. The three surfaces obtained for each glycopeptide model were virtually identical, corroborating that
Fitting of Raw ab initio Data to Periodic Equations. The periodicity of the surface indicates that functions that reproduces the topology of the chemical shift surfaces could in principle be estimated. Following the methodology of Oldfield and coworkers,6
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