Article
Properties of Escherichia coli EF-Tu mutants designed for fluorescence resonance energy transfer from tRNA molecules.
Protein engineering, design & selection : PEDS - 1 Mar 2010
Perla-Kajan Joanna, Lin Xin, Cooperman Barry S, Goldman Emanuel, Jakubowski Hieronim, Knudsen Charlotte R, Mandecki Wlodek
Abstract excerpt
Here we describe the design, preparation and characterization of 10 EF-Tu mutants of potential utility for the study of Escherichia coli elongation factor Tu (EF-Tu) interaction with tRNA by a fluorescence resonance energy transfer assay. Each mutant contains a single cysteine residue at positions in EF-Tu that are proximal to tRNA sites within the aminoacyl-tRNA.EF-Tu.GTP ternary complex that have previously...
Topics
- Binding Sites
- Electrophoretic Mobility Shift Assay
- Escherichia coli
- Factor Xa
- Fluorescence Resonance Energy Transfer
- Guanosine Diphosphate
- Hydrolysis
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutant Proteins
- Mutation
- Nucleic Acid Conformation