Article
The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability.
Journal of biochemical and biophysical methods - 3 Jan 2000
Vorstenbosch E L, Potapov A P, de Graaf J M, Kraal B
Abstract excerpt
Elongation factor Tu is essential for binding and a correct delivery of aminoacyl-tRNA during protein biosynthesis. For a good characterization of its interaction with tRNA in terms of structure-function relationship, determinations of kinetic equilibrium parameters are of great value. We describe two novel methods for that purpose. One method is based on EF-Tu protection of the tRNA 3' acceptor end against RNase...
Topics
- Binding, Competitive
- Biochemistry
- Guanosine Diphosphate
- Guanosine Triphosphate
- Histidine
- Models, Chemical
- Mutation
- Peptide Elongation Factor Tu
- Peptides
- RNA, Transfer, Amino Acyl
- RNA, Transfer, Phe
- Recombinant Proteins
- Reproducibility of Results
- Ribonuclease, Pancreatic