Globular Proteins: Difference between revisions
No edit summary |
No edit summary |
||
| Line 41: | Line 41: | ||
* <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. | ||
* <scene name='Globular_Proteins/Protein_l9/1'>Ribosomal protein L9</scene> - from | * <scene name='Globular_Proteins/Protein_l9/1'>Ribosomal protein L9</scene> - from B. stearothermophillus, a prokayote. The length of the long α-helix is invariant with other prokayotic L9 proteins. | ||
* <scene name='Globular_Proteins/Flavodxin/1'>Flavodoxin</scene> - This type of structure is also called doubly wound parallel β-sheet because of the loops of α-helices on both sides of the sheet. In some cases these doubly wound sheets contain a few antiparallel strands forming a mixed β-sheet. Can you find the three layers of backbone in these doubly wound sheets contain? | * <scene name='Globular_Proteins/Flavodxin/1'>Flavodoxin</scene> - This type of structure is also called doubly wound parallel β-sheet because of the loops of α-helices on both sides of the sheet. In some cases these doubly wound sheets contain a few antiparallel strands forming a mixed β-sheet. Can you find the three layers of backbone in these doubly wound sheets contain? | ||
* <scene name='Globular_Proteins/Pg_mutase/1'>Phosphoglycerate mutase</scene> - There is one antiparallel strand in the sheet, and the double winding is more extensive. | * <scene name='Globular_Proteins/Pg_mutase/1'>Phosphoglycerate mutase</scene> - There is one antiparallel strand in the sheet, and the double winding is more extensive. | ||
* <scene name='Globular_Proteins/Rnase/1'>Ribonuclease H</scene> - endoribonuclease from ''E. coli'' that cleaves the RNA strand of a RNA:DNA duplex and produces oligonucleotides. This activity is involved in bacterial replication and required for retrovirial infection. The ''E. coli'' enzyme is homologous with retrovirial proteins. | * <scene name='Globular_Proteins/Rnase/1'>Ribonuclease H</scene> - endoribonuclease from ''E. coli'' that cleaves the RNA strand of a RNA:DNA duplex and produces oligonucleotides. This activity is involved in bacterial replication and required for retrovirial infection. The ''E. coli'' enzyme is homologous with retrovirial proteins. | ||
* <scene name='Globular_Proteins/Ruva/1'>RuvA protein</scene> - ''E. coli'' that binds DNA along with RuvB, a helicase, and both are involved in DNA repair, SOS response and DNA recombination. Residues 143-156 are misssing. | * <scene name='Globular_Proteins/Ruva/1'>RuvA protein</scene> - ''E. coli'' protein that binds DNA along with RuvB, a helicase, and both are involved in DNA repair, SOS response and DNA recombination. Residues 143-156 are misssing. | ||