1
It is composed of a short alpha-helix and a three-stranded antiparallel beta-sheet.
2
The structure is comprised of a central antiparallel beta-sheet flanked on both sides by alpha-helices.
3
The protein contains one alpha-helix and two strands of antiparallel beta-sheet, with a type IV beta-turn connecting the two strands.
4
The structure is characterized by 2 segments of alpha-helices and a triple-stranded antiparallel beta-sheet stabilized by 4 disulfide bridges.
5
From these data, it is apparent that self-assembly involves the formation of antiparallel beta-sheets and pi-pi-stacking.
6
The secondary structure contains one alpha-helix and eight beta-strands, seven of which are arranged in two contiguous, antiparallel beta-sheets.