Abstract
The conformation in solution of the biantennary complex type oligosaccharide unit derived from human serotransferrin has been investigated using 1H— 1H Nuclear Overhauser Effect (NOE) measurements at 300 MHz. From quantitation of the NOE, the α(1–3) antenna is shown to exist in a preferred solution conformation with respect to the mannosyl-chitobiose core. The flexibility of the α(1–6) arm, together with the absence of NOE data between this arm and the core, indicates that, in contrast to the α(1–3) arm the α(1–6) arm has no preferred conformation with respect to the core.
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