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Bacteriorhodopsin barrel proteins

Membranes contain many largely a-helical proteins. Cell surface receptors often appear to have one, two, or several membrane-spanning helices (see Chapter 8). The single peptide chain of the bacterial light-operated ion pump bacteriorhodopsin (Fig. 23-45) folds back upon itself to form seven helical rods just long enough to span the bacterial membrane in which it functions.189 Photosynthetic reaction centers contain an a helix bundle which is formed from two different protein subunits (Fig. 23-31).190 A recently discovered a,a barrel contains 12 helices. Six parallel helices form an inner barrel and 6 helices antiparallel to the first 6 form an outer layer (see Fig. 2-29).191-193... [Pg.71]

Figure 4 Two examples of membrane proteins, (a) Bacteriorhodopsin is mainly an a-protein containing seven helices. It is a membrane protein serving as an ion pump and is found in bacteria that can survive in high salt concentrations, (b) Porin is a P-barrel. Porins work as channels in cell membranes, which let small metabolites such as ions and amino acids in and out of the cell. Figure drawn using MOLSCRIPT. ... Figure 4 Two examples of membrane proteins, (a) Bacteriorhodopsin is mainly an a-protein containing seven helices. It is a membrane protein serving as an ion pump and is found in bacteria that can survive in high salt concentrations, (b) Porin is a P-barrel. Porins work as channels in cell membranes, which let small metabolites such as ions and amino acids in and out of the cell. Figure drawn using MOLSCRIPT. ...

See other pages where Bacteriorhodopsin barrel proteins is mentioned: [Pg.132]    [Pg.21]    [Pg.38]    [Pg.127]    [Pg.518]   


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