This page contains all the figures used in the notes on beta sheets. You may want to keep this page open, or print this page when going through the notes. Please note that the sheet molecluar visualisations (Figures 2.1 and 2.5) are kept on a different page to avoid long download times.
Figure 2.2 Antiparallel beta sheet
The diagram on the left shows how the alternate strands run in opposite direction to each other and the hydrogen bonds connecting the strands (dotted lines). The diagram on the right indicates that the strands can be far apart in the polypeptide chain and can be separated by a long, or short, intervening connection. These intervening connections may consist of helices, other strands, turns or any other secondary structures.
The diagram on the left shows how the alternate strands run in the same direction to each other and the hydrogen bonds connecting the strands (dotted lines). The diagram on the right indicates that the strands can be far apart in the polypeptide chain and can be separated by a long, or short, intervening connection. These intervening connections may consist of helices, other strands, turns or any other secondary structures.
Figure 2.4 Twists in beta sheets
The diagram shows the twist of a beta sheet in carboxypeptidase A (5cpa.pdb).
'Top view' of beta sheet
'Side view' of the beta sheet shown above showing the pronounced twist
Figure 2.5 Beta sheets in OmpF (Outer membrane protein F)
This figure shows three examples of beta bulges which are irregularities found in antiparallel beta sheets and which break hydrogen bonds between strands in a sheet.
Adopted from Richardson. J.S. (1981) Advances in Protein Chemistry 34:167-339
