Electron Paramagnetic Resonance Study of the Mixed-Valent Diiron Center in Escherichia coli Ribonucleotide Reductase Produced by Reduction of Radical-Free Protein R2 at 77 K

1994 ◽  
Vol 116 (24) ◽  
pp. 11120-11128 ◽  
Author(s):  
Roman Davydov ◽  
Sergei Kuprin ◽  
Astrid Graeslund ◽  
Anders Ehrenberg
Keyword(s):  
Escherichia Coli ◽  
Electron Paramagnetic Resonance ◽  
Ribonucleotide Reductase ◽  
Electron Paramagnetic Resonance Study ◽  
Paramagnetic Resonance ◽  
Free Protein ◽  
Electron Paramagnetic

Interaction of selectively spin-labeled 70S ribosomes with tRNAPhe. An electron paramagnetic resonance study

1981 ◽  
Vol 59 (5) ◽  
pp. 311-314 ◽  
Author(s):  
Angel Rodriguez ◽  
Hermann Dugas
Keyword(s):  
Escherichia Coli ◽  
Electron Paramagnetic Resonance ◽  
Structural Change ◽  
Ribosomal Proteins ◽  
Electron Paramagnetic Resonance Study ◽  
Paramagnetic Resonance ◽  
Trna Molecule ◽  
Sh Groups ◽  
Ribosome Structure ◽  
Electron Paramagnetic

70S ribosomes from Escherichia coli, selectively spin labeled on the SH groups of proteins S18, S12, S21, S17, and L27, were used to study the formation of the tertiary complex ribosome–poly(U)–tRNAPhe. Most of these ribosomal proteins are located in the region of binding of tRNA. The electron paramagnetic resonance observable structural change suggests a loosening of the ribosome structure upon binding of the tRNA molecule.

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