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Ruth M Saecker

Showing results (11-20 of 27) with videos related to

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Methods in Enzymology|January 10, 2004
Rapid quench mixing to quantify kinetics of steps in association of Escherichia coli RNA polymerase with promoter DNARuth M Saecker, Oleg V Tsodikov, Michael W Capp, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 1, 2005
The effects of upstream DNA on open complex formation by Escherichia coli RNA polymeraseCaroline A Davis, Michael W Capp, M Thomas Record, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 2, 2007
Real-time footprinting of DNA in the first kinetically significant intermediate in open complex formation by Escherichia coli RNA polymeraseCaroline A Davis, Craig A Bingman, Robert Landick, et al.
Biochemistry|February 16, 2006
Solute probes of conformational changes in open complex (RPo) formation by Escherichia coli RNA polymerase at the lambdaPR promoter: evidence for unmasking of the active site in the isomerization step and for large-scale coupled folding in the subsequent conversion to RPoWayne S Kontur, Ruth M Saecker, Caroline A Davis, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 21, 2010
One-step DNA melting in the RNA polymerase cleft opens the initiation bubble to form an unstable open complexTheodore J Gries, Wayne S Kontur, Michael W Capp, et al.
Biochemistry|March 6, 2010
Probing DNA binding, DNA opening, and assembly of a downstream clamp/jaw in Escherichia coli RNA polymerase-lambdaP(R) promoter complexes using salt and the physiological anion glutamateWayne S Kontur, Michael W Capp, Theodore J Gries, et al.
Journal of Molecular Biology|June 11, 2002
Kinetic studies and structural models of the association of E. coli sigma(70) RNA polymerase with the lambdaP(R) promoter: large scale conformational changes in forming the kinetically significant intermediatesRuth M Saecker, Oleg V Tsodikov, Kristi L McQuade, et al.
Journal of Molecular Biology|November 4, 2008
Evidence for a tyrosine-adenine stacking interaction and for a short-lived open intermediate subsequent to initial binding of Escherichia coli RNA polymerase to promoter DNALisa A Schroeder, Theodore J Gries, Ruth M Saecker, et al.
Biochemistry|November 17, 2004
Preferential interactions of glycine betaine and of urea with DNA: implications for DNA hydration and for effects of these solutes on DNA stabilityJiang Hong, Michael W Capp, Charles F Anderson, et al.
Biochemistry|September 18, 2009
Interactions of the osmolyte glycine betaine with molecular surfaces in water: thermodynamics, structural interpretation, and prediction of m-valuesMichael W Capp, Laurel M Pegram, Ruth M Saecker, et al.
Pageof 3

Showing results (11-20 of 27) with videos related to

Sort By:
Pageof 3
Methods in Enzymology|January 10, 2004
Rapid quench mixing to quantify kinetics of steps in association of Escherichia coli RNA polymerase with promoter DNARuth M Saecker, Oleg V Tsodikov, Michael W Capp, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 1, 2005
The effects of upstream DNA on open complex formation by Escherichia coli RNA polymeraseCaroline A Davis, Michael W Capp, M Thomas Record, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 2, 2007
Real-time footprinting of DNA in the first kinetically significant intermediate in open complex formation by Escherichia coli RNA polymeraseCaroline A Davis, Craig A Bingman, Robert Landick, et al.
Biochemistry|February 16, 2006
Solute probes of conformational changes in open complex (RPo) formation by Escherichia coli RNA polymerase at the lambdaPR promoter: evidence for unmasking of the active site in the isomerization step and for large-scale coupled folding in the subsequent conversion to RPoWayne S Kontur, Ruth M Saecker, Caroline A Davis, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 21, 2010
One-step DNA melting in the RNA polymerase cleft opens the initiation bubble to form an unstable open complexTheodore J Gries, Wayne S Kontur, Michael W Capp, et al.
Biochemistry|March 6, 2010
Probing DNA binding, DNA opening, and assembly of a downstream clamp/jaw in Escherichia coli RNA polymerase-lambdaP(R) promoter complexes using salt and the physiological anion glutamateWayne S Kontur, Michael W Capp, Theodore J Gries, et al.
Journal of Molecular Biology|June 11, 2002
Kinetic studies and structural models of the association of E. coli sigma(70) RNA polymerase with the lambdaP(R) promoter: large scale conformational changes in forming the kinetically significant intermediatesRuth M Saecker, Oleg V Tsodikov, Kristi L McQuade, et al.
Journal of Molecular Biology|November 4, 2008
Evidence for a tyrosine-adenine stacking interaction and for a short-lived open intermediate subsequent to initial binding of Escherichia coli RNA polymerase to promoter DNALisa A Schroeder, Theodore J Gries, Ruth M Saecker, et al.
Biochemistry|November 17, 2004
Preferential interactions of glycine betaine and of urea with DNA: implications for DNA hydration and for effects of these solutes on DNA stabilityJiang Hong, Michael W Capp, Charles F Anderson, et al.
Biochemistry|September 18, 2009
Interactions of the osmolyte glycine betaine with molecular surfaces in water: thermodynamics, structural interpretation, and prediction of m-valuesMichael W Capp, Laurel M Pegram, Ruth M Saecker, et al.
Pageof 3