Pub. Date : 1997 Aug 19
PMID : 9254632
9 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Crystallographic investigations have revealed that EF-G.GDP resembles the EF-Tu.GTP. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |
| 2 | However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |
| 3 | However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |
| 4 | However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |
| 5 | However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |
| 6 | However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |
| 7 | However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |
| 8 | However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |
| 9 | The small-angle X-ray scattering study described here was undertaken to ascertain if the form of EF-G that has high ribosome affinity, EF-G.GTP, the structure of which is unknown, could be a mimic of EF-Tu.GDP. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |