Relative orientation of close-packed β-pleated sheets in proteins

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Abstract
When .beta.-pleated sheets pack face to face in proteins, the angle between the strand directions of the 2 .beta.-sheets is observed to be near -30.degree.. A simple model is proposed for .beta.-sheet-to-.beta.-sheet packing in concanavalin A, plastocyanin, .gamma.-crystallin, superoxide dismutase, prealbumin and the immunoglobin fragment VREI. This model shows how the observed relative orientation of 2 packed .beta.-sheets is a consequence of the rows of side chains at the interace being approximately aligned and the .beta.-sheet having a right-handed twist. The special amino acid composition of residues at the .beta.-sheet-to-.beta.-sheet interfaces makes the contact surfaces essentially smooth and hydrophobic.