Globular Proteins: Difference between revisions
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* <scene name='Globular_Proteins/Lectin_r_s/1'>Lectin</scene> - from ''R. solanacearum''. It is an example of a protein having a quaternary structure, in this case it is trimeric - <scene name='Globular_Proteins/Lectin_r_s2/1'>three subunits</scene>. This type of structure is called a six-bladed propellor or β-propellor. Each subunit contributes two propellors. | * <scene name='Globular_Proteins/Lectin_r_s/1'>Lectin</scene> - from ''R. solanacearum''. It is an example of a protein having a quaternary structure, in this case it is trimeric - <scene name='Globular_Proteins/Lectin_r_s2/1'>three subunits</scene>. This type of structure is called a six-bladed propellor or β-propellor. Each subunit contributes two propellors. | ||
==== Mixed | ==== Mixed helices and β-Sheets ==== | ||
* <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''. 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, which contact water, 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/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, which contact water, 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. | ||
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* <scene name='Globular_Proteins/Insulin1/1'>Insulin</scene> - Among its functions is the regulation of glucose uptake by cells. The small peptide contains A and B chains that are connected by disulfide bonds, and the tertiary structure of the A chain is also held in place by a disulfide bond. | * <scene name='Globular_Proteins/Insulin1/1'>Insulin</scene> - Among its functions is the regulation of glucose uptake by cells. The small peptide contains A and B chains that are connected by disulfide bonds, and the tertiary structure of the A chain is also held in place by a disulfide bond. | ||
* <scene name='Globular_Proteins/Crambin/1'>Crambin</scene> - Plant seed peptide. Small single chain peptide with no significant backbone layers but has disulfide bonds to stabilize the tertiary structure. Disulfide bonds, also, have an important role of keeping the relatively high proportion of loops in place. | * <scene name='Globular_Proteins/Crambin/1'>Crambin</scene> - Plant seed peptide. Small single chain peptide with no significant backbone layers but has disulfide bonds to stabilize the tertiary structure. Disulfide bonds, also, have an important role of keeping the relatively high proportion of loops in place. | ||
* <scene name='Globular_Proteins/Pholipase2/1'>Phospholipase A2</scene> - Part of a class of hydrolases that degrade glycerophospholipids. This one specifically hydrolyzes the second acyl group on the glycero group. This example is larger than the other two, but it still does not have well organized backbone layers in part due to the extensive loops. | * <scene name='Globular_Proteins/Pholipase2/1'>Phospholipase A2</scene> - Part of a class of hydrolases that degrade glycerophospholipids. This one specifically hydrolyzes the second acyl group on the glycero group. This example is larger than the other two, but it still does not have well organized backbone layers in part due to the extensive turns and loops. | ||
=== Metal-Rich Proteins === | === Metal-Rich Proteins === | ||