Theoretical studies on protein-nucleic acid interactions. II. Hydrogen bonding of amino acid side chains with bases and base pairs of nucleic acids

Biopolymers ◽  
1984 ◽  
Vol 23 (10) ◽  
pp. 1995-2008 ◽  
Author(s):  
N. Vasant Kumar ◽  
Girjesh Govil
2003 ◽  
Vol 327 (4) ◽  
pp. 781-796 ◽  
Author(s):  
Alan C. Cheng ◽  
William W. Chen ◽  
Cynthia N. Fuhrmann ◽  
Alan D. Frankel

2011 ◽  
Vol 109 (16) ◽  
pp. 1995-2008 ◽  
Author(s):  
P. Deepa ◽  
P. Kolandaivel ◽  
K. Senthilkumar

FEBS Letters ◽  
1973 ◽  
Vol 30 (2) ◽  
pp. 219-224 ◽  
Author(s):  
H. Sellini ◽  
J.C. Maurizot ◽  
J.L. Dimicoli ◽  
C. Helene

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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