Globular Proteins: Difference between revisions
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==== Mixed α-helix and β-Sheet ==== | ==== Mixed α-helix and β-Sheet ==== | ||
* <scene name='Globular_Proteins/Tmvp2/1'>Tobacco mosaic virus protein</scene> - forms the capsid of the virus. Again the α-helices, loops and turns are prominent features, and the α-helices are antiparallel. | * <scene name='Globular_Proteins/Tmvp2/1'>Tobacco mosaic virus protein</scene> - forms the capsid of the virus. Again the α-helices, loops and turns are prominent features, and the α-helices are antiparallel. | ||
* <scene name='Globular_Proteins/Porin/1'>Matrix porin</scene> - integral protein from the outer membrane of ''E. coli''. | * <scene name='Globular_Proteins/Porin/1'>Matrix porin</scene> - integral protein from the outer membrane of ''E. coli''. Since the barrel structure is inserted into the interior of the membrane, the outer surface that contacts the membrane must be largely <scene name='Globular_Proteins/Porin_phobic/1'>hydrophobic</scene>, but the ends and much of the interior is <scene name='Globular_Proteins/Porin_polar/1'>polar</scene>. <scene name='Globular_Proteins/Porin_polar_phobic/1'>Both</scene> shown together. | ||
* <scene name='Globular_Proteins/Concan/1'>Concanavalin</scene> - Example of another lectin. Notice that the tertiary structures of the three lectins are different revealing that the structures can be different but yet have the same general function. There are two antiparallel β-sheets with the hydrophobic sides of the sheets facing each other. They are interlocking β-Sheets or have Greek Key Topology, ''i.e.'' after laying down a strand in a sheet, often the peptide chain loops over to the other sheet and lays down a strand in that sheet. | * <scene name='Globular_Proteins/Concan/1'>Concanavalin</scene> - Example of another lectin. Notice that the tertiary structures of the three lectins are different revealing that the structures can be different but yet have the same general function. There are two antiparallel β-sheets with the hydrophobic sides of the sheets facing each other. They are interlocking β-Sheets or have Greek Key Topology, ''i.e.'' after laying down a strand in a sheet, often the peptide chain loops over to the other sheet and lays down a strand in that sheet. | ||
* <scene name='Globular_Proteins/Crystallin/1'>Gamma-Crystallin</scene> - A protein that is a component of the eye lense. This protein is another example of interlocking β-sheet, two of the Greek key bilayers are connected by a looping peptide segment. | * <scene name='Globular_Proteins/Crystallin/1'>Gamma-Crystallin</scene> - A protein that is a component of the eye lense. This protein is another example of interlocking β-sheet, two of the Greek key bilayers are connected by a looping peptide segment. | ||