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Biophysical Chemistry|September 23, 2003
Preferential interactions in aqueous solutions of urea and KClJiang Hong, Michael W Capp, Charles F Anderson, et al.
Nucleic Acids Research|October 17, 2017
The mechanism and high-free-energy transition state of lac repressor-lac operator interactionRituparna Sengupta, Michael W Capp, Irina A Shkel, 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 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.
Journal of Molecular Biology|June 10, 2015
E. coli RNA Polymerase Determinants of Open Complex Lifetime and StructureEmily F Ruff, Amanda C Drennan, Michael W Capp, et al.
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