Contemporary glycobiology reflects the intense interest in glycoproteins and their biological roles. Addition of saccharides by N- or O-glycosylation is precise rather than random and forms a uniquely interactive molecular surface. We designate these well conserved glycomotifs as glycomodules to emphasize their functional significance. Thus, elucidation of the glycosylation codes that determine saccharide addition is a significant goal. The focus here is on the Hyp O-glycosylation of cell wall proteins. This involves two consecutive posttranslational modifications, proline hydroxylation and glycosylation. Peptide sequence rather than conformation seems to determine these modifications. Hyp glycosylation occurs in two distinct modes: Hyp arabinosylation and Hyp galactosylation. The Hyp contiguity hypothesis predicts arabinosylation of contiguous Hyp residues and galactosylation of clustered non-contiguous Hyp. Elucidation of Hyp glycosylation codes involves the design and expression of putative glycomotifs as simple repetitive peptides. Thus, repetitive (Ser-Hyp), directed Hyp galactosylation resulting in the exclusive addition of arabinogalactan polysaccharide to all the non-contiguous Hyp residues. and a new AGP. Another repetitive peptide from gum arabic glycoprotein, containing both contiguous and non-contiguous Hyp, directed both modes of Hyp glycosylation. Furthermore, expression of the (Ser-Hypx)n series confirmed the arabinosylation of contiguous Hyp. Thus, the Hyp contiguity hypothesis is a useful predictive tool in the functional genomics toolbox.