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Showing results (41-50 of 78) with videos related to

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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.
Journal of Bacteriology|August 23, 2006
Crowding and confinement effects on protein diffusion in vivoMichael C Konopka, Irina A Shkel, Scott Cayley, et al.
Biochemistry|March 14, 2018
Quantifying Interactions of Nucleobase Atoms with Model Compounds for the Peptide Backbone and Glutamine and Asparagine Side Chains in WaterXian Cheng, Irina A Shkel, Cristen Molzahn, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 12, 2011
Separation of preferential interaction and excluded volume effects on DNA duplex and hairpin stabilityD B Knowles, Andrew S LaCroix, Nickolas F Deines, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 18, 2013
Probing the protein-folding mechanism using denaturant and temperature effects on rate constantsEmily J Guinn, Wayne S Kontur, Oleg V Tsodikov, 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.
Biochemistry|August 6, 2013
Quantifying additive interactions of the osmolyte proline with individual functional groups of proteins: comparisons with urea and glycine betaine, interpretation of m-valuesRoger C Diehl, Emily J Guinn, Michael W Capp, 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.
Proceedings of the National Academy of Sciences of the United States of America|September 21, 2011
Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizerEmily J Guinn, Laurel M Pegram, Michael W Capp, et al.
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Showing results (41-50 of 78) with videos related to

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Pageof 8
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.
Journal of Bacteriology|August 23, 2006
Crowding and confinement effects on protein diffusion in vivoMichael C Konopka, Irina A Shkel, Scott Cayley, et al.
Biochemistry|March 14, 2018
Quantifying Interactions of Nucleobase Atoms with Model Compounds for the Peptide Backbone and Glutamine and Asparagine Side Chains in WaterXian Cheng, Irina A Shkel, Cristen Molzahn, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 12, 2011
Separation of preferential interaction and excluded volume effects on DNA duplex and hairpin stabilityD B Knowles, Andrew S LaCroix, Nickolas F Deines, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 18, 2013
Probing the protein-folding mechanism using denaturant and temperature effects on rate constantsEmily J Guinn, Wayne S Kontur, Oleg V Tsodikov, 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.
Biochemistry|August 6, 2013
Quantifying additive interactions of the osmolyte proline with individual functional groups of proteins: comparisons with urea and glycine betaine, interpretation of m-valuesRoger C Diehl, Emily J Guinn, Michael W Capp, 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.
Proceedings of the National Academy of Sciences of the United States of America|September 21, 2011
Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizerEmily J Guinn, Laurel M Pegram, Michael W Capp, et al.
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