scholarly journals PAQMAN: Protein-nucleic acid affinity quantification by MAss spectrometry in nuclear extracts

Methods ◽  
2020 ◽  
Vol 184 ◽  
pp. 70-77 ◽  
Author(s):  
Cathrin Gräwe ◽  
Matthew M. Makowski ◽  
Michiel Vermeulen
Methods ◽  
2018 ◽  
Vol 144 ◽  
pp. 64-78 ◽  
Author(s):  
M. Scalabrin ◽  
S.M. Dixit ◽  
M.M. Makshood ◽  
C.E. Krzemien ◽  
Daniele Fabris

Author(s):  
Stephen D. Jett

The electrophoresis gel mobility shift assay is a popular method for the study of protein-nucleic acid interactions. The binding of proteins to DNA is characterized by a reduction in the electrophoretic mobility of the nucleic acid. Binding affinity, stoichiometry, and kinetics can be obtained from such assays; however, it is often desirable to image the various species in the gel bands using TEM. Present methods for isolation of nucleoproteins from gel bands are inefficient and often destroy the native structure of the complexes. We have developed a technique, called “snapshot blotting,” by which nucleic acids and nucleoprotein complexes in electrophoresis gels can be electrophoretically transferred directly onto carbon-coated grids for TEM imaging.


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