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The conformational statistics of the glycosylated dipeptides N acetyl - y - 0 - (2 - acetamido - a - D - galactopyranosyl) - L seryl - N - methyl amide and its threonyl analog (galNAc Ser/Thr) as models of O-linked glycopeptides were determined using umbrella sampling. The use of umbrella sampling allowed the importance sampling algorithm to accept new conformations with probabilities of 32% and 24%, respectively. More vigorous movement from one conformation to another produces a chain of conformations and a set of properties suitable for comparison with experimental results where available. The O-linked glycopeptides exhibited substantial steric hindrance. The serine linkage compound preferred an amino acid polpyproline conformation. The presence of the methyl group in the threonine side chain inverted the relative distribution of amino acid

Conformational statistics of models for serine- and threonine-linked glycopeptides using umbrella sampling