Structure of maltoheptaose by difference Fourier methods and a model for glycogen

The structure of the glucose heptamer, maltoheptaose, has been determined by difference Fourier analysis at 0.25 nm resolution through its binding to phosphorylase a. It is a left-handed helical structure, with 6.5 glucose residues per turn and a rise per residue of 2.4 Å. The molecule shows short-range order when no protein is present to stabilize its conformation in solution. With one exception, the individual torsion angles between sugar residues vary over a narrow range and preserve a good O₍₂₎O_(3′) hydrogen bond. The length of an individual chain for glycogen can be extrapolated from the maltoheptaose data and agrees well with the size for glycogen predicted by the Whelan model.