Radiolytic protein surface mapping.
We report that high energy beta particles may function as a means for mapping the surface of a protein. Comparable to Fe-EDTA in the presence of ascorbate and peroxide, 90Y-EDTA alone can break polypeptide backbone bonds on the surface of E. coli RNA polymerase. The two methods give very similar fragmentation patterns, although some unique fragments are produced by each. Radiolytic footprinting may prove useful for mapping proteins inside living cells, since beta-radiolysis produces reactive species up to approximately 1 cm away from the emitting 90Y.
Greiner
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DP
Department of Chemistry, University of California, Davis 95616, USA.
Hughes
K A
KA
Meares
C F
CF
D001610:Beta Particles; D055592:Biophysical Phenomena; D001703:Biophysics; D002614:Chelating Agents; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry* / Q000528:radiation effects*; D004492:Edetic Acid; D004926:Escherichia coli / Q000201:enzymology; D011506:Proteins / Q000737:chemistry* / Q000528:radiation effects*; D013499:Surface Properties; D015021:Yttrium Radioisotopes
D002614:Chelating Agents; D011506:Proteins; D015021:Yttrium Radioisotopes; D004492:Edetic Acid; D012321:DNA-Directed RNA Polymerases