A recurring organization of protein secondary structure elements in three dimensions. Structural-cluster counts depend on comparison criteria and should not automatically be equated to counts of distinct topological folds.
A beta sheet closed into a barrel-like protein fold by joining its edge strands through backbone hydrogen bonds. A membrane-spanning barrel can present nonpolar side chains to lipid while lining a pore with polar groups; soluble barrels instead have a different solvent-facing pattern. The topology alone does not imply a membrane location.
The predominantly alpha-helical structural framework characteristic of globins. Conserved haem-pocket architecture in myoglobin and haemoglobin supplies evidence for divergence from a shared ancestor.

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