Protein folds In the alpha + beta class
I. alpha-helices on one side of a beta-sheet

High-energy phosphate carrier from the phosphotransferase system of E. coli.
The fold shown here exploits the common beta-alpha-beta motif in which an aalpha-ehelix lines up in a parallel fashion with two beta strands.
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           (for all models).
  Heat shock protein 90. Hsp 90 molecular chaperones play essential roles in the folding and activation of a range of client proteins involved in cell cycle regulation and signal transduction in eukaryotic cells.
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