Effects of Kirromycin on the Elongation Factor EF-Tu and its Interactions with GDP or GTP and tRNA. The Application of zone-Interference Gel Electrophoresis, a New Method for the Analysis of Weak Complexes
All the members of the GTP-binding protein family behave like molecular switches. They can have two conformations: in the presence of bound GTP the complex is in the “on” conformation and, after GTP hydrolysis, the GDP containing complex is in the “off” position. The switching process can become blocked by natural ways, such as phosphorylation or ADP-ribosylation, as well as by artificial tricks, such as mutagenesis at strategic positions of the protein chain or by the use of non-hydrolyzable GTP-analogues.
KeywordsWeak Complex High Negative Charge tRNA Molecule Ribosomal Complex Intrinsic GTPase Activity
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