Analytical Ultracentrifugation for Analysis of Protein–Nucleic Acid Interactions

2021 ◽  
pp. 397-421
Author(s):  
Andrea Bogutzki ◽  
Ute Curth
Keyword(s):  
Nucleic Acid ◽  
Analytical Ultracentrifugation ◽  
Protein Nucleic Acid ◽  
Nucleic Acid Interactions

The shock of the old: hydrodynamics for the masses

2008 ◽  
Vol 36 (4) ◽  
pp. 766-770 ◽  
Author(s):  
David J. Scott
Keyword(s):  
Nucleic Acid ◽  
Molecular Biology ◽  
Analytical Ultracentrifugation ◽  
Statistical Thermodynamics ◽  
Low Concentrations ◽  
Subunit Stoichiometry ◽  
Protein Nucleic Acid ◽  
The Masses ◽  
Nucleic Acid Interactions

Hydrodynamic techniques such as analytical ultracentrifugation can provide key information about subunit stoichiometry and interaction strengths of protein–nucleic acid interactions. Analysis is complicated by (i) the need for low concentrations in order to observe both free and bound species and (ii) thermodynamic non-ideality. With the introduction of fluorescence optics, we are able to obtain data at lower concentrations, and improved understanding of the statistical thermodynamics of macromolecular solutions has allowed non-ideality to be accurately assigned. With these developments, it is possible now to assay protein–nucleic acid interactions at concentrations typically used in molecular biology assays.

Snapshot blotting: The transfer of nucleic acids and nucleoprotein complexes from electrophoresis gels to EM grids

1992 ◽  
Vol 50 (1) ◽  
pp. 762-763
Author(s):  
Stephen D. Jett
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acids ◽  
Nucleic Acid Binding ◽  
Mobility Shift ◽  
Carbon Coated ◽  
Nucleoprotein Complexes ◽  
Mobility Shift Assay ◽  
Protein Nucleic Acid ◽  
Gel Mobility Shift ◽  
Nucleic Acid Interactions

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.

Use of difference boundary sedimentation velocity to investigate nonspecific protein-nucleic acid interactions

Biochemistry ◽  
1980 ◽  
Vol 19 (15) ◽  
pp. 3516-3522 ◽  
Author(s):  
Timothy M. Lohman ◽  
C. Glen Wensley ◽  
Jeffrey Cina ◽  
Richard R. Burgess ◽  
M. Thomas Record
Keyword(s):  
Nucleic Acid ◽  
Sedimentation Velocity ◽  
Protein Nucleic Acid ◽  
Nucleic Acid Interactions

Protein—nucleic acid interactions Folding and binding Web alert

1998 ◽  
Vol 8 (1) ◽  
pp. 9-10 ◽  
Author(s):  
PhilipE Bourne ◽  
Judith Murray-Rust ◽  
JeremyH Lakey
Keyword(s):  
Nucleic Acid ◽  
Protein Nucleic Acid ◽  
Nucleic Acid Interactions

Nonspecific Prion Protein–Nucleic Acid Interactions Lead to Different Aggregates and Cytotoxic Species

Biochemistry ◽  
2012 ◽  
Vol 51 (27) ◽  
pp. 5402-5413 ◽  
Author(s):  
Bruno Macedo ◽  
Thiago A. Millen ◽  
Carolina A. C. A. Braga ◽  
Mariana P. B. Gomes ◽  
Priscila S. Ferreira ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Prion Protein ◽  
Protein Nucleic Acid ◽  
Nucleic Acid Interactions

Visualization of protein-nucleic acid interactions in a virus

1989 ◽  
Vol 208 (2) ◽  
pp. 307-325 ◽  
Author(s):  
Keiichi Namba ◽  
Rekha Pattanayek ◽  
Gerald Stubbs
Keyword(s):  
Nucleic Acid ◽  
Protein Nucleic Acid ◽  
Nucleic Acid Interactions
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